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蛋白质纤维的制备方法与流程

文档序号:24941345发布日期:2021-05-04 11:34
蛋白质纤维的制备方法与流程
本发明涉及一种蛋白质纤维的制备方法。
背景技术
:以往,作为含有结构蛋白质并以此为主要成分的蛋白质纤维的制备方法,已知有一种用于将从喷嘴喷出的纺丝原液在凝固浴中凝固而形成纤维的湿式纺丝法及干湿式纺丝法。在蛋白质纤维的湿式纺丝法及干湿式纺丝法中,报道了使用将蛋白质溶解在溶剂中的蛋白质溶液作为纺丝原液(纺液),将纺丝原液从喷嘴挤出到凝固液中以使溶剂从纺丝原液中脱去,并且形成纤维以作为未拉伸丝,从而可以得到蛋白质纤维(例如,参照专利文献1、专利文献2、非专利文献1以及非专利文献2)。作为制备蛋白质纤维时用于凝固液的溶剂,通常可以使用甲醇、乙醇、2-丙醇等低级醇、以及丙酮等酮类。非专利文献1报道了例如,将再生蚕丝蛋白(再生蚕丝丝心蛋白)溶解于甲酸中,导入低级醇或丙酮的凝固液,形成再生蚕丝丝心蛋白纤维的方法、以及非专利文献2等报道了将具有来自于nephilaclavipesmasp1的氨基酸序列的蛛丝类丝心蛋白溶解在六氟异丙醇(hfip)中,并将其导入到甲醇的凝固液中以形成蛛丝类丝心蛋白纤维的方法。现有技术文献专利文献专利文献1:日本特许第5540154号公报专利文献2:日本特许第5584932号公报非专利文献非专利文献1::int.j.biol.macromol.,34卷,2004年,pp.89-105非专利文献2:pnas,august10,2010,vol.107,no.32,pp.14059-14063发明概要发明所要解决的课题当使用作为将来利用价值高的材料的高分子量的结构蛋白质,例如蚕丝丝心蛋白、蛛丝类丝心蛋白、以及角蛋白等,通过湿式纺丝法以及干湿式纺丝法制备蛋白质纤维时,用于形成蛋白质纤维的凝固液非常有限。其中,甲醇、乙醇、2-丙醇等低级醇、以及丙酮等酮类能够以比较低的价格获得,并且具有纤维形成能力,因此作为结构蛋白质的凝固液而被广泛使用。但是,这些凝固溶剂被指定为消防法中的第4类危险物,具有爆炸、发生火灾等危险性,从安全性的观点来看,作为制备工序中消耗量最大的凝固溶剂,很难说是合适的。从制造成本及环境负荷的观点来看,也希翼进一步降低负荷。鉴于上述现有技术的问题,本发明的目的在于提供一种蛋白质纤维的制备方法,其使用含有水或水溶液的凝固液进行制备。用于解决课题的方案本发明人等为了解决上述现有技术的课题而反复进行了深入研究。结果发现,可以通过将含有蛋白质及有机溶剂的纺丝原液与含有水或ph为0.25以上且ph为10.00以下的水溶液的凝固液组合,来制备蛋白质纤维。即,本发明涉及例如以下各发明。[1]一种蛋白质纤维的制备方法,其中,包括使含有蛋白质和有机溶剂的纺丝原液与凝固液接触,并且使上述蛋白质凝固的工序,以纺丝原液总量为基准,上述纺丝原液中的上述蛋白质含量大于10质量%,上述凝固液含有水或ph为0.25以上且ph为10.00以下的水溶液。[2]根据[1]所述的方法,其中,以上述凝固液的总量为基准,上述凝固液中的水或水溶液的含量为60质量%以上。[3]根据[1]或[2]所述的方法,其中,上述水溶液为盐水溶液、酸水溶液或其混合溶液。[4]根据[3]所述的方法,其中,上述酸水溶液为羧酸水溶液。[5]根据[3]或[4]所述的方法,其中,以上述凝固液的总量为基准,上述凝固液中的盐含量为0.1质量%以上。[6]根据[5]所述的方法,其中,上述盐包括选自由羧酸盐及无机盐构成的组中的至少1种。[7]根据[6]所述的方法,其中,上述无机盐包括选自由硫酸盐、氯化物、硝酸盐、碘化物盐、碳酸盐、硫酸氢盐、磷酸氢盐、碳酸氢盐及硫氰酸盐构成的组中的至少1种。[8]根据[6]或[7]所述的方法,其中,上述无机盐包括选自由硫酸盐、氯化物、磷酸氢盐及碳酸氢盐构成的组中的至少1种。[9]根据[7]或[8]所述的方法,其中,上述氯化物包括选自由氯化钠、氯化钙、氯化铵、氯化钾、氯化锂、氯化镁及氯化胍构成的组中的至少1种。[10]根据[7]至[9]中任意所述的方法,其中,上述硫酸盐包括选自由硫酸铵、硫酸钾、硫酸钠、硫酸锂、硫酸镁及硫酸钙构成的组中的至少1种。[11]根据[3]至[10]中任意所述的方法,其中,上述盐水溶液包括选自由硫酸钠水溶液、氯化钠水溶液、微咸水及海水构成的组中的至少1种。[12]根据[3]至[11]中任意所述的方法,其中,以上述凝固液中的上述盐水溶液和溶解于上述凝固液中的上述有机溶剂的总含量为100质量%计,从与凝固液接触的纺丝原液溶解于上述凝固液中的有机溶剂的含量为40质量%以下。[13]根据[1]至[12]中任意所述的方法,其中,上述蛋白质的平均疏水性指标大于-1.3。[14]根据[1]至[13]中任意所述的方法,其中,上述蛋白质包括选自由蜘蛛丝蛋白、丝蛋白、胶原蛋白、节肢弹性蛋白、弹性蛋白、角蛋白构成的组中的至少1种。[15]根据[1]至[14]中任意所述的方法,其中,上述蛋白质是角蛋白或蜘蛛丝蛋白。[16]根据[1]至[15]中任意所述的方法,其中,上述蛋白质是蜘蛛丝蛋白。[17]根据[1]至[16]中任意所述的方法,其中,上述蛋白质的平均疏水性指标大于-0.8。[18]根据[1]至[17]中任意所述的方法,其中,还具备拉伸凝固的蛋白质的工序。[19]根据[1]至[18]中任意所述的方法,其中,上述有机溶剂包含选自由甲酸、二甲基亚砜及六氟异丙醇构成的组中的至少1种。[20]根据[1]至[19]中任意一项所述的方法,其中,上述有机溶剂包含选自由甲酸及二甲基亚砜构成的组中的至少1种。[21]根据[1]至[20]中任意所述的方法,其中,上述纺丝原液还含有溶解促进剂。[22]一种蛋白质纤维的制备方法,其中,包括使含有蛋白质及溶剂的纺丝原液与凝固液接触,并且使上述蛋白质凝固的工序,以纺丝原液总量为基准,上述纺丝原液中的上述蛋白质含量大于10质量%,上述凝固液含有水或ph为0.25以上且ph为2.50以下或ph为7.50以上且ph为10.00以下的的水溶液。发明效果根据本发明,可以提供一种蛋白质纤维的制备方法,其使用含有水或水溶液的凝固液进行制备。通过使用含有水或水溶液的凝固液,可以降低爆炸、发生火灾等的危险性、制造成本以及环境负荷。附图说明图1是表示蛛丝类丝心蛋白的结构域序列的一例的示意图。图2是表示蛛丝类丝心蛋白的结构域序列的一例的示意图。图3是表示蛛丝类丝心蛋白的结构域序列的一例的示意图。图4是示意性地表示用于制备蛋白质纤维的纺丝装置的一例的说明图。图5是表示吸湿发热性能试验的结果的一例的图表。具体实施方式下面,将对本发明的实施方式进行详细说明。但是,本发明并不限于以下实施方式。(蛋白质纤维的制备方法)本实施方式的蛋白质纤维的制备方法包括使含有蛋白质及有机溶剂的纺丝原液与凝固液接触,并且使蛋白质凝固的工序。在此,以纺丝原液总量为基准,纺丝原液中的蛋白质含量大于10质量%。此外,凝固液含有水或ph为0.25以上且ph为10.00以下的水溶液。本实施方式的蛋白质纤维的制备方法可以根据湿式纺丝、干湿式纺丝等公知的纺丝方法来来进行。<纺丝原液>本实施方式所涉及的纺丝原液含有蛋白质及有机溶剂。(蛋白质)根据本实施方式的制备方法来制备的蛋白质纤维含有蛋白质并以此作为主要成分。本实施方式的纺丝原液中所含的蛋白质是人工制备的蛋白质(人造蛋白质),而并不是天然蛋白质或其纯化产物。对于人工制备蛋白质的方法并没有特别限定,可以是通过基因重组技术利用微生物等来进行制备,也可以是通过合成来进行制备。上述蛋白质例如可以是结构蛋白质或来自于该结构蛋白质的人造结构蛋白质。所谓结构蛋白质,是指在生物体内形成或保持结构、形态等的蛋白质。作为结构蛋白质,例如,可以列举出蜘蛛丝蛋白(蛛丝类丝心蛋白等)、丝蛋白、胶原蛋白、节肢弹性蛋白、弹性蛋白、角蛋白等。本实施方式的蜘蛛丝蛋白包括天然来源的蜘蛛丝蛋白和修饰的蜘蛛丝蛋白(以下也称为“修饰丝心蛋白”)。在本说明书中,所谓“天然来源的蜘蛛丝蛋白”,是指具有与天然来源的蜘蛛丝蛋白(蛛丝类丝心蛋白等)相同的氨基酸序列的蜘蛛丝蛋白,所谓“修饰的蜘蛛丝蛋白”或“修饰丝心蛋白”,是指具有与天然来源的蜘蛛丝蛋白不同的氨基酸序列的蜘蛛丝蛋白。作为天然来源的蜘蛛丝蛋白,例如,可以列举出大吐丝管牵引丝蛋白、横丝蛋白以及小壶状腺丝蛋白等蛛丝类所产生的蛛丝类丝心蛋白。大吐丝管牵引丝具有由结晶区域和非晶区域(也称为无定形区域)构成的重复区域,因此兼具较高的应力和伸缩性。蜘蛛丝的横丝具有如下特征:虽不具有结晶区域,但是具有由非晶区域构成的重复区域。横丝与大吐丝管牵引丝相比,应力差但具有较高的伸缩性。大吐丝管牵引丝蛋白由蜘蛛的大壶状腺产生,具有强韧性优异的特征。作为大吐丝管牵引丝蛋白,例如可以列举出来自于金纺蜘蛛(nephilaclavipes)的大壶状腺丝蛋白masp1及masp2、以及来自于十字园蛛(araneusdiadematus)的adf3及adf4。adf3是十字园蛛的2种主要牵引丝蛋白之一。蜘蛛丝蛋白也可以是来自于这些牵引丝蛋白的蜘蛛丝蛋白。来自于adf3的蜘蛛丝蛋白比较容易合成,并且在强伸度及韧性方面具有优异的特性。横丝蛋白是由蜘蛛的鞭状腺(flagelliformgland)产生的。作为横丝蛋白,例如可以列举出来自于金纺蜘蛛(nephilaclavipes)的鞭毛状腺丝蛋白(flagelliformsilkprotein)。作为蛛丝类所产生的蛛丝类丝心蛋白的另一个例子,例如,可以列举出鬼蛛、十字园蛛、肥胖园蛛、五纹园蛛及大腹圆蛛等属于园蛛属(araneus属)的蜘蛛、青新园蛛、嗜水新园蛛、灌木新园蛛及类青新园蛛等属于新园蛛属(neoscona属)的蜘蛛、棕类岬蛛等属于岬蛛属(pronus属)的蜘蛛、蟾蜍曲腹蛛及对称曲腹蛛等属于曲腹蛛属(cyrtarachne属)的蜘蛛、库氏棘腹蛛及乳突棘腹蛛等属于棘腹蛛属(gasteracantha属)的蜘蛛、何氏瘤腹蛛及六刺瘤腹蛛等属于瘤腹蛛属(ordgarius属)的蜘蛛、悦目金蛛、小悦目金蛛及横纹金蛛等属于金蛛属(argiope属)的蜘蛛、双峰尾园蛛等属于尾园蛛属(arachnura属)的蜘蛛、褐吊叶蛛等属于吊叶蛛属(acusilas属)的蜘蛛、摩鹿加云斑蛛、方格云斑蛛及全色云斑蛛等属于云斑蛛属(cytophora属)的蜘蛛、丑锥头蛛等属于锥头蛛属(poltys属)的蜘蛛、八疣尘蛛、四突尘蛛、圆腹尘蛛及黑尾尘蛛等属于尘蛛属(cyclosa属)的蜘蛛及日本壮头蛛等属于壮头蛛属(chorizopes属)的蜘蛛所产生的蜘蛛丝蛋白、以及前齿肖蛸、锥腹肖蛸、直伸肖蛸及鳞纹肖蛸等属于肖蛸属(tetragnatha属)的蜘蛛、纵条银鳞蛛、肩斑银鳞蛛及小肩斑银鳞蛛等属于银鳞蛛属(leucauge属)的蜘蛛、棒络新妇及斑络新妇等属于络新妇属(nephila属)的蜘蛛、美丽麦蛛等属于麦蛛属(menosira属)的蜘蛛、柔弱粗螯蛛等属于锯螯蛛属(dyschiriognatha属)的蜘蛛、黑寡妇蜘蛛、红背蜘蛛、几何寇蛛及间斑寇蛛等属于寇蛛属(latrodectus属)的蜘蛛、以及属于育儿网蛛属(euprosthenops属)的蜘蛛等属于肖蛸科(tetragnathidae科)的蜘蛛所产生的蜘蛛丝蛋白。作为蛛丝类所产生的蜘蛛丝蛋白的更具体的例子,例如,可以列举出fibroin-3(adf-3)[来自于araneusdiadematus](genbank登录号aac47010(氨基酸序列)、u47855(碱基序列))、fibroin-4(adf-4)[来自于araneusdiadematus](genbank登录号aac47011(氨基酸序列)、u47856(碱基序列))、draglinesilkproteinspidroin1[来自于nephilaclavipes](genbank登录号aac04504(氨基酸序列)、u37520(碱基序列))、majorampullatespidroin1[来自于latrodectushesperus](genbank登录号abr68856(氨基酸序列)、ef595246(碱基序列))、draglinesilkproteinspidroin2[来自于nephilaclavata](genbank登录号aal32472(氨基酸序列)、af441245(碱基序列))、majorampullatespidroin1[来自于euprosthenopsaustralis](genbank登录号caj00428(氨基酸序列)、aj973155(碱基序列))、以及majorampullatespidroin2[euprosthenopsaustralis](genbank登录号cam32249.1(氨基酸序列)、am490169(碱基序列))、minorampullatesilkprotein1[nephilaclavipes](genbank登录号aac14589.1(氨基酸序列))、minorampullatesilkprotein2[nephilaclavipes](genbank登录号aac14591.1(氨基酸序列))、minorampullatespidroin-likeprotein[nephilengyscruentata](genbank登录号abr37278.1(氨基酸序列)等。本实施方式的蜘蛛丝蛋白例如可以为包含式1:[(a)n基序-rep]m、或式2:[(a)n基序-rep]m-(a)n基序所示的结构域序列的蛋白质。本实施方式的蜘蛛丝蛋白可以在结构域序列的n末端侧及c末端侧中的任意一个或两个中进一步添加有氨基酸序列(n末端序列及c末端序列)。n末端序列及c末端序列并不限定于此,通常为不具有丝心蛋白中的特征性的氨基酸基序的重复的区域,并且由100个残基左右的氨基酸构成。在本说明书中,所谓“结构域序列”,为生成丝心蛋白特有的结晶区域(典型地,相当于氨基酸序列的(a)n基序)和非晶区域(典型地,相当于氨基酸序列的rep)的氨基酸序列,并且是指式1:[(a)n基序-rep]m、或式2:[(a)n基序-rep]m-(a)n基序所示的氨基酸序列。在此,(a)n基序表示以丙氨酸残基为主的氨基酸序列,并且氨基酸残基数为2~27。(a)n基序的氨基酸残基数可以为2~20、4~27、4~20、8~20、10~20、4~16、8~16或10~16。此外,(a)n基序中的丙氨酸残基数相对于氨基酸残基总数的比例只要为40%以上即可,可以为60%以上、70%以上、80%以上、83%以上、85%以上、86%以上、90%以上、95%以上或100%(意味着仅由丙氨酸残基构成)。在结构域序列中存在的多个(a)n基序中的至少7个可以仅由丙氨酸残基构成。rep表示由2~200个氨基酸残基构成的氨基酸序列。rep可以是由10~200个氨基酸残基构成的氨基酸序列,也可以是由10~40、10~60、10~80、10~100、10~120、10~140、10~160或10~180个氨基酸残基构成的氨基酸序列。m表示2~300的整数,可以是8~300、10~300、10~300、20~300、40~300、60~300、80~300、10~200、20~200、20~180、20~160、20~140或20~120的整数。存在的多个(a)n基序可以是彼此相同的氨基酸序列,也可以是彼此不同的氨基酸序列。存在的多个rep可以是彼此相同的氨基酸序列,也可以是彼此不同的氨基酸序列。修饰的蜘蛛丝蛋白(修饰丝心蛋白)例如可以为依据天然来源的蛛丝类丝心蛋白的氨基酸序列对其氨基酸序列进行修饰而得到的蜘蛛丝蛋白(例如,通过对克隆出的天然来源的蛛丝类丝心蛋白的基因序列进行修饰来修饰氨基酸序列而得到的蜘蛛丝蛋白),而且也可以为不依赖于天然来源的蛛丝类丝心蛋白而人工设计及合成的蜘蛛丝蛋白(例如,通过对编码所设计的氨基酸序列的核酸进行化学合成而具有所希望的氨基酸序列的蜘蛛丝蛋白)。另外,在本实施方式中,作为修饰丝心蛋白,由于保温性能、吸湿发热性能及/或阻燃性能也很优异,因此优选使用修饰蛛丝类丝心蛋白。例如可以通过对克隆出的天然来源的蛛丝类丝心蛋白的基因序列进行例如与置换、缺失、插入及/或添加一个或多个氨基酸残基相当的氨基酸序列的修饰,从而可以得到修饰丝心蛋白。氨基酸残基的置换、缺失、插入及/或添加可以通过局部特异性突变法等本领域技术人员熟知的方法来进行。具体而言,可以根据nucleicacidres.10,6487(1982)、methodsinenzymology,100,448(1983)等文献中记载的方法来进行。作为修饰丝心蛋白的具体实施例,可以列举出来自于蜘蛛的大壶状腺所产生的大吐丝管牵引丝蛋白的修饰丝心蛋白(第1修饰丝心蛋白)、降低了甘氨酸残基的含量的修饰丝心蛋白(第2修饰丝心蛋白)、降低了(a)n基序的含量的修饰丝心蛋白(第3修饰丝心蛋白)、降低了甘氨酸残基的含量及(a)n基序的含量的修饰丝心蛋白(第4修饰丝心蛋白)、具有局部包含疏水性指标大的区域的结构域序列的修饰丝心蛋白(第5修饰丝心蛋白)、及具有降低了谷氨酰胺残基的含量的结构域序列的修饰丝心蛋白(第6修饰丝心蛋白)。作为来自于蜘蛛的大壶状腺所产生的大吐丝管牵引丝蛋白的修饰丝心蛋白(第1修饰丝心蛋白),可以列举出包含式1:[(a)n基序-rep]m所示的结构域序列的蛋白质。在第1修饰丝心蛋白中,式1中的n优选为3~20的整数,更优选为4~20的整数,进一步优选为8~20的整数,更进一步优选为10~20的整数,进一步还优选为4~16的整数,特别优选为8~16的整数,最优选为10~16的整数。在第1修饰丝心蛋白中,式1中构成rep的氨基酸残基数优选为10~200个残基,更优选为10~150个残基,进一步优选为20~100个残基,更进一步优选为20~75个残基。在第1修饰丝心蛋白中,式1:[(a)n基序-rep]m所示的氨基酸序列所含的甘氨酸残基、丝氨酸残基及丙氨酸残基的合计残基数相对于氨基酸残基总数优选为40%以上,更优选为60%以上,进一步优选为70%以上。第1修饰丝心蛋白可以为以下这种蛋白质:包含式1:[(a)n基序-rep]m所示的氨基酸序列的单元,并且c末端序列为序列号1~3中任意一个所示的氨基酸序列、或与序列号1~3中任意一个所示的氨基酸序列具有90%以上的同源性的氨基酸序列。序列号1所示的氨基酸序列与由adf3(gi:1263287、ncbi)的氨基酸序列的c末端的50个残基的氨基酸构成的氨基酸序列相同,序列号2所示的氨基酸序列与从序列号1所示的氨基酸序列的c末端除去20个残基后的氨基酸序列相同,序列号3所示的氨基酸序列与从序列号1所示的氨基酸序列的c末端除去29个残基后的氨基酸序列相同。作为第1修饰丝心蛋白的更具体的例子,可以列举出包括与(1-i)序列号4所示的氨基酸序列、或(1-ii)序列号4所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列的修饰丝心蛋白。序列一致性优选为95%以上。序列号4所示的氨基酸序列为在n末端添加有由起始密码子、his10标签及hrv3c蛋白酶(humanrhinovirus3c蛋白酶)识别位点构成的氨基酸序列(序列号5)的adf3的氨基酸序列中,以使第1~13位的重复区域增加为约2倍、并且在第1154位氨基酸残基处终止翻译的方式突变后得到。序列号4所示的氨基酸序列的c末端的氨基酸序列与序列号3所示的氨基酸序列相同。(1-i)的修饰丝心蛋白可以由序列号4所示的氨基酸序列构成。降低了甘氨酸残基的含量的修饰丝心蛋白(第2修饰丝心蛋白)具有其结构域序列与天然来源的蛛丝类丝心蛋白相比甘氨酸残基的含量降低的氨基酸序列。第2修饰丝心蛋白与天然来源的蛛丝类丝心蛋白相比,可以具有与至少rep中的一个或多个甘氨酸残基被置换为其他氨基酸残基相当的氨基酸序列。第2修饰丝心蛋白的结构域序列与天然来源的蛛丝类丝心蛋白相比,在rep中的选自ggx及gpgxx(其中,g表示甘氨酸残基,p表示脯氨酸残基,x表示甘氨酸以外的氨基酸残基)中的至少一种基序序列中,可以具有相当于至少一个或多个该基序序列中的一个甘氨酸残基被置换为其他氨基酸残基的氨基酸序列。第2修饰丝心蛋白中,上述甘氨酸残基被置换为其他氨基酸残基的基序序列的比例相对于全部基序序列可以为10%以上。第2修饰丝心蛋白包括式1:[(a)n基序-rep]m所示的结构域序列并且具有下述氨基酸序列:当将从上述结构域序列中除去自位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列后得到的序列中的全部rep所包含的由xgx(其中,x表示甘氨酸以外的氨基酸残基)构成的氨基酸序列的氨基酸残基总数设为z、并且将从上述结构域序列中除去自位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列后得到的序列中的氨基酸残基总数设为w时,z/w可以为30%以上、40%以上、50%以上或50.9%以上。(a)n基序中的丙氨酸残基数相对于氨基酸残基总数可以为83%以上,优选为86%以上,更优选为90%以上,进一步优选为95%以上,更进一步优选为100%(意味着仅由丙氨酸残基构成)。第2修饰丝心蛋白优选地通过将ggx基序中的一个甘氨酸残基置换为其他氨基酸残基来提高由xgx构成的氨基酸序列的含有比例。在第2修饰丝心蛋白中,结构域序列中的由ggx构成的氨基酸序列的含有比例优选为30%以下,更优选为20%以下,进一步优选为10%以下,更进一步优选为6%以下,进一步还优选为4%以下,特别优选为2%以下。结构域序列中的由ggx构成的氨基酸序列的含有比例可以通过与下述的由xgx构成的氨基酸序列的含有比例(z/w)的计算方法相同的方法来计算。对z/w的计算方法进一步进行详细说明。首先,在包含式1:[(a)n基序-rep]m所示的结构域序列的蛛丝类丝心蛋白(修饰丝心蛋白或天然来源的蛛丝类丝心蛋白)中,从由结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列所含的全部rep中,提取由xgx构成的氨基酸序列。构成xgx的氨基酸残基的总数为z。例如,当提取了50个由xgx构成的氨基酸序列时(没有重复),z为50×3=150。此外,例如,如由xgxgx构成的氨基酸序列的情况那样,当包含在2个xgx中的x(中间的x)存在时,通过扣除重复部分来进行计算(当为xgxgx时,为5个氨基酸残基)。w为从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列所含的氨基酸残基总数。例如,当为图1所示的结构域序列时,w为4+50+4+100+4+10+4+20+4+30=230(除去位于最靠c末端侧的(a)n基序)。然后,通过将z除以w,可以计算出z/w(%)。在第2修饰丝心蛋白中,z/w优选为50.9%以上,更优选为56.1%以上,进一步优选为58.7%以上,更进一步优选为70%以上,进一步还优选为80%以上。z/w的上限并没有特别限制,例如可以为95%以下。例如可以通过如下方式进行修饰而获得第2修饰丝心蛋白:从克隆出的天然来源的蛛丝类丝心蛋白的基因序列中,对编码甘氨酸残基的碱基序列的至少一部分进行置换并使其编码其他氨基酸残基。此时,作为修饰的甘氨酸残基,可以选择ggx基序及gpgxx基序中的一个甘氨酸残基、另外也可以用将z/w设定为50.9%以上的方式进行置换。此外,例如,也可以通过根据天然来源的蛛丝类丝心蛋白的氨基酸序列设计满足上述方式的氨基酸序列,并通过对编码所设计的氨基酸序列的核酸进行化学合成后得到。在任何一种情况下,除了与在从天然来源的蛛丝类丝心蛋白的氨基酸序列中将rep中的甘氨酸残基置换为其他氨基酸残基相当的修饰之外,还可以进一步进行与置换、缺失、插入及/或添加一个或多个氨基酸残基相当的氨基酸序列的修饰。作为上述的其他氨基酸残基,只要是除甘氨酸残基以外的氨基酸残基即可,并没有特别限制,优选缬氨酸(v)残基、亮氨酸(l)残基、异亮氨酸(i)残基、蛋氨酸(m)残基、脯氨酸(p)残基、苯丙氨酸(f)残基及色氨酸(w)残基等疏水性氨基酸残基、谷氨酰胺(q)残基、天冬酰胺(n)残基、丝氨酸(s)残基、赖氨酸(k)残基及谷氨酸(e)残基等亲水性氨基酸残基,更优选缬氨酸(v)残基、亮氨酸(l)残基、异亮氨酸(i)残基及谷氨酰胺(q)残基,进一步优选谷氨酰胺(q)残基。作为第2修饰丝心蛋白的更具体的例子,可以列举出包括与(2-i)序列号6、序列号7、序列号8或序列号9所示的氨基酸序列、或者(2-ii)序列号6、序列号7、序列号8或序列号9所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列的修饰丝心蛋白。对(2-i)的修饰丝心蛋白进行说明。序列号6所示的氨基酸序列通过将相当于将天然来源的蛛丝类丝心蛋白的序列号10所示的氨基酸序列的rep中的所有ggx置换为gqx而得到。序列号7所示的氨基酸序列通过在序列号6所示的氨基酸序列中从n末端侧向c末端侧使(a)n基序每隔2个发生缺失,并进一步在c末端序列的近前插入一个[(a)n基序-rep]而得到。序列号8所示的氨基酸序列在序列号7所示的氨基酸序列的各个(a)n基序的c末端侧插入2个丙氨酸残基,进一步将部分谷氨酰胺(q)残基置换为丝氨酸(s)残基、并且使n末端侧的部分氨基酸缺失以使得其与序列号7的分子量几乎相同。序列号9所示的氨基酸序列在将序列号11所示的氨基酸序列中存在的20个结构域序列的区域(其中,该区域的c末端侧的数个氨基酸残基被置换)重复4次后的序列的c末端中添加his标签。序列号10所示的氨基酸序列(相当于天然来源的蛛丝类丝心蛋白)中的z/w的值为46.8%。序列号6所示的氨基酸序列、序列号7所示的氨基酸序列、序列号8所示的氨基酸序列及序列号9所示的氨基酸序列中的z/w的值分别为58.7%、70.1%、66.1%及70.0%。此外,序列号10、序列号6、序列号7、序列号8及序列号9所示的氨基酸序列的锯齿比率(在下文中说明)为1:1.8~11.3的x/y的值分别为15.0%、15.0%、93.4%、92.7%及89.3%。(2-i)的修饰丝心蛋白可以由序列号6、序列号7、序列号8或序列号9所示的氨基酸序列构成。(2-ii)的修饰丝心蛋白包括与序列号6、序列号7、序列号8或序列号9所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列。(2-ii)的修饰丝心蛋白也为包含式1:[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95%以上。(2-ii)的修饰丝心蛋白与序列号6、序列号7、序列号8或序列号9所示的氨基酸序列具有90%以上的序列一致性,并且当将rep中所含的由xgx(其中,x表示甘氨酸以外的氨基酸残基)构成的氨基酸序列的氨基酸残基总数设为z、将上述结构域序列中的rep的氨基酸残基总数设为w时,z/w优选为50.9%以上。第2修饰丝心蛋白可以在n末端及c末端中的任意一端或两端包含标签序列。由此,可以实现修饰丝心蛋白的分离、固定、检测及可视化等。作为标签序列,例如,可以列举出利用了与其他分子的特异性亲和性(结合性、亲和性)的亲和性标签。作为亲和性标签的具体实施例,可以列举出组氨酸标签(his标签)。his标签是由4至10个左右的组氨酸残基排列而成的短肽,具有与镍等的金属离子特异性结合的性质,因此可以用于通过金属螯合层析(chelatingmetalchromatography)进行的修饰丝心蛋白的分离。作为标签序列的具体实施例,例如,可以列举出序列号12所示的氨基酸序列(包含his标签序列及铰链序列的氨基酸序列)。此外,也可以利用与谷胱甘肽特异性结合的谷胱甘肽-s-转移酶(gst)、与麦芽糖特异性结合的麦芽糖结合蛋白(mbp)等标签序列。更进一步地,还可以使用利用了抗原抗体反应的“表位标签”。通过添加用于显示抗原性的肽(表位)作为标签序列,可以结合针对该表位的抗体。作为表位标签,可以列举出ha(流感病毒血凝素的肽序列)标签、myc标签、flag标签等。通过利用表位标签,可以很容易地以高特异性对修饰丝心蛋白进行纯化。更进一步地,也可以使用利用特定的蛋白酶将标签序列切除而得到的标签。也可以通过对经由该标签序列吸附的蛋白质进行蛋白酶处理,来回收切除标签序列后的修饰丝心蛋白。作为含有标签序列的第2修饰丝心蛋白的更具体的例子,可以列举出包括与(2-iii)序列号13、序列号11、序列号14或序列号15所示的氨基酸序列、或(2-iv)序列号13、序列号11、序列号14或序列号15所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列的修饰丝心蛋白。序列号16、序列号17、序列号13、序列号11、序列号14及序列号15所示的氨基酸序列分别在序列号10、序列号18、序列号6、序列号7、序列号8及序列号9所示的氨基酸序列的n末端添加序列号12所示的氨基酸序列(包含his标签序列及铰链序列)。(2-iii)的修饰丝心蛋白可以由序列号13、序列号11、序列号14或序列号15所示的氨基酸序列构成。(2-iv)的修饰丝心蛋白包括与序列号13、序列号11、序列号14或序列号15所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列。(2-iv)的修饰丝心蛋白也为包含式1:[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95%以上。(2-iv)的修饰丝心蛋白与序列号13、序列号11、序列号14或序列号15所示的氨基酸序列具有90%以上的序列一致性,并且当将rep中所含的由xgx(其中,x表示甘氨酸以外的氨基酸残基)构成的氨基酸序列的氨基酸残基总数设为z、将上述结构域序列中的rep的氨基酸残基总数设为w时,z/w优选为50.9%以上。第2修饰丝心蛋白可以含有用于将重组蛋白生产系统所生产的蛋白质释放到宿主外部的分泌信号。分泌信号的序列可以根据宿主的种类来进行适当设定。降低了(a)n基序的含量的修饰丝心蛋白(第3修饰丝心蛋白)具有其结构域序列与天然来源的蛛丝类丝心蛋白相比(a)n基序的含量降低的氨基酸序列。第3修饰丝心蛋白的结构域序列与天然来源的蛛丝类丝心蛋白相比,具有相当于缺失了至少一个或多个(a)n基序的氨基酸序列。第3修饰丝心蛋白可以具有相当于从天然来源的蛛丝类丝心蛋白中缺失了10~40%的(a)n基序的氨基酸序列。第3修饰丝心蛋白的结构域序列与天然来源的蛛丝类丝心蛋白相比,其可以至少从n末端侧向c末端侧具有相当于每1~3个(a)n基序中缺失一个(a)n基序的氨基酸序列。第3修饰丝心蛋白的结构域序列与天然来源的蛛丝类丝心蛋白相比,其可以至少从n末端侧向c末端侧具有相当于依次重复发生了2个连续的(a)n基序的缺失及一个(a)n基序的缺失的氨基酸序列。第3修饰丝心蛋白的结构域序列可以至少从n末端侧向c末端侧具有相当于每隔2个发生一次缺失(a)n基序的氨基酸序列。第3修饰丝心蛋白包括式1:[(a)n基序-rep]m所示的结构域序列并且具有下述氨基酸序列:从n末端侧向c末端侧依次比较相邻的2个[(a)n基序-rep]单元的rep的氨基酸残基数,将氨基酸残基数少的rep的氨基酸残基数设为1时,并且将另一个rep的氨基酸残基数的比为1.8~11.3的相邻的2个[(a)n基序-rep]单元的氨基酸残基数相加而得到的合计值的最大值设为x、将结构域序列的氨基酸残基总数设为y时,x/y为20%以上、30%以上、40%以上或50%以上。(a)n基序中的丙氨酸残基数相对于氨基酸残基总数可以为83%以上,优选为86%以上,更优选为90%以上,进一步优选为95%以上,更进一步优选为100%(意味着仅由丙氨酸残基构成)。参照图1进一步地详细说明x/y的计算方法。图1示出了从蛛丝类丝心蛋白中除去n末端序列及c末端序列后的结构域序列。该结构域序列从n末端侧(左侧)起具有(a)n基序-第1rep(50个氨基酸残基)-(a)n基序-第2rep(100个氨基酸残基)-(a)n基序-第3rep(10个氨基酸残基)-(a)n基序-第4rep(20个氨基酸残基)-(a)n基序-第5rep(30个氨基酸残基)-(a)n基序的序列。以不重复的方式从n末端侧向c末端侧依次选择相邻的2个[(a)n基序-rep]单元。此时,也可以存在未被选择的[(a)n基序-rep]单元。图1示出了模式1(第1rep与第2rep的比较、以及第3rep与第4rep的比较)、模式2(第1rep与第2rep的比较、以及第4rep与第5rep的比较)、模式3(第2rep与第3rep的比较、以及第4rep与第5rep的比较)、模式4(第1rep与第2rep的比较)。另外,除此之外还存在选择方法。接下来,对于各模式,比较所选择的相邻的2个[(a)n基序-rep]单元中的各rep的氨基酸残基数。通过求出将氨基酸残基数相对较少的一方设为1时的另一方的氨基酸残基数的比来进行比较。例如,在比较第1rep(50个氨基酸残基)和第2rep(100个氨基酸残基)的情况下,当将氨基酸残基数相对较少的第1rep设为1时,第2rep的氨基酸残基数的比为100/50=2。同样地,在比较第4rep(20个氨基酸残基)和第5rep(30个氨基酸残基)的情况下,当将氨基酸残基数相对较少的第4rep设为1时,第5rep的氨基酸残基数的比为30/20=1.5。图1中,用实线表示当将氨基酸残基数相对较少的一方设为1时,另一方的氨基酸残基数的比为1.8~11.3的[(a)n基序-rep]单元的组。下面将这样的比称为锯齿比率。用虚线表示当将氨基酸残基数相对较少的一方设为1时,另一方的氨基酸残基数的比小于1.8或大于11.3的[(a)n基序-rep]单元的组。在各个模式中,将实线所示的相邻的2个[(a)n基序-rep]单元的所有氨基酸残基数相加(不仅仅是rep,也是(a)n基序的氨基酸残基数。)。而且,将相加后的合计值进行比较,并将该合计值最大的模式的合计值(合计值的最大值)设为x。在图1所示的例子中,模式1的合计值最大。接下来,可以通过将x除以结构域序列的氨基酸残基总数y来计算出x/y(%)。在第3修饰丝心蛋白中,x/y优选为50%以上,更优选为60%以上,进一步优选为65%以上,更进一步优选为70%以上,进一步还优选为75%以上,特别优选为80%以上。x/y的上限并没有特别限制,例如可以为100%以下。当锯齿比率为1:1.9~11.3时,x/y优选为89.6%以上,当锯齿比率为1:1.8~3.4时,x/y优选为77.1%以上,当锯齿比率为1:1.9~8.4时,x/y优选为75.9%以上,当锯齿比率为1:1.9~4.1时,x/y优选为64.2%以上。当第3修饰丝心蛋白为在结构域序列中存在多个(a)n基序中的至少7个仅由丙氨酸残基构成的修饰丝心蛋白时,x/y优选为46.4%以上,更优选为50%以上,进一步优选为55%以上,更进一步优选为60%以上,进一步还优选为70%以上,特别优选为80%以上。x/y的上限并没有特别限制,为100%以下即可。例如可以通过从克隆出的天然来源的蛛丝类丝心蛋白的基因序列中,以将x/y设为64.2%以上的方式使编码(a)n基序的序列中的一个或多个缺失,从而得到第3修饰丝心蛋白。此外,例如也可以通过设计出相当于从天然来源的蛛丝类丝心蛋白的氨基酸序列中,以将x/y设为64.2%以上的方式使一个或多个(a)n基序发生缺失的氨基酸序列,并且对编码所设计的氨基酸序列的核酸进行化学合成后得到。在任何情况下,除了与在从天然来源的蛛丝类丝心蛋白的氨基酸序列中缺失(a)n基序相当的修饰之外,还可以进一步进行与置换、缺失、插入及/或添加一个或多个氨基酸残基相当的氨基酸序列的修饰。作为第3修饰丝心蛋白的更具体的例子,可以列举出包括与(3-i)序列号18、序列号7、序列号8或序列号9所示的氨基酸序列、或者(3-ii)序列号18、序列号7、序列号8或序列号9所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列的修饰丝心蛋白。对(3-i)的修饰丝心蛋白进行说明。序列号18所示的氨基酸序列通过在相当于天然来源的蛛丝类丝心蛋白的序列号10所示的氨基酸序列中从n末端侧向c末端侧使(a)n基序每隔2个发生缺失,并进一步在c末端序列的近前插入一个[(a)n基序-rep]而得到。序列号7所示的氨基酸序列通过将序列号18所示的氨基酸序列的rep中的所有ggx置换为gqx而得到。序列号8所示的氨基酸序列在序列号7所示的氨基酸序列的各个(a)n基序的c末端侧插入2个丙氨酸残基,进一步将部分谷氨酰胺(q)残基置换为丝氨酸(s)残基、并且使n末端侧的部分氨基酸缺失以使得其与序列号7的分子量几乎相同。序列号9所示的氨基酸序列在将序列号11所示的氨基酸序列中存在的20个结构域序列的区域(其中,该区域的c末端侧的数个氨基酸残基被置换)重复4次后的序列的c末端中添加his标签。序列号10所示的氨基酸序列(相当于天然来源的蛛丝类丝心蛋白)的锯齿比率为1:1.8~11.3中的x/y的值为15.0%。序列号18所示的氨基酸序列及序列号7所示的氨基酸序列中的x/y的值均为93.4%。序列号8所示的氨基酸序列中的x/y的值为92.7%。序列号9所示的氨基酸序列中的x/y的值为89.3%。序列号10、序列号18、序列号7、序列号8及序列号9所示的氨基酸序列中的z/w的值分别为46.8%、56.2%、70.1%、66.1%及70.0%。(3-i)的修饰丝心蛋白可以由序列号18、序列号7、序列号8或序列号9所示的氨基酸序列构成。(3-ii)的修饰丝心蛋白包括与序列号18、序列号7、序列号8或序列号9所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列。(3-ii)的修饰丝心蛋白也为包含式1:[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95%以上。(3-ii)的修饰丝心蛋白与序列号18、序列号7、序列号8或序列号9所示的氨基酸序列具有90%以上的序列一致性,并且从n末端侧向c末端侧依次比较相邻的2个[(a)n基序-rep]单元的rep的氨基酸残基数,将氨基酸残基数少的rep的氨基酸残基数设为1时,并且将另一个rep的氨基酸残基数的比为1.8~11.3(锯齿比率为1:1.8~11.3)的相邻的2个[(a)n基序-rep]单元的氨基酸残基数相加而得到的合计值的最大值设为x、将结构域序列的氨基酸残基总数设为y时,x/y优选为64.2%以上。第3修饰丝心蛋白可以在n末端及c末端中的任意一端或两端包含上述标签序列。作为含有标签序列的第3修饰丝心蛋白的更具体的例子,可以列举出包括与(3-iii)序列号17、序列号11、序列号14或序列号15所示的氨基酸序列、或(3-iv)序列号17、序列号11、序列号14或序列号15所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列的修饰丝心蛋白。序列号16、序列号17、序列号13、序列号11、序列号14及序列号15所示的氨基酸序列分别在序列号10、序列号18、序列号6、序列号7、序列号8及序列号9所示的氨基酸序列的n末端添加序列号12所示的氨基酸序列(包含his标签序列及铰链序列)。(3-iii)的修饰丝心蛋白可以由序列号17、序列号11、序列号14或序列号15所示的氨基酸序列构成。(3-iv)的修饰丝心蛋白包括与序列号17、序列号11、序列号14或序列号15所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列。(3-iv)的修饰丝心蛋白也为包含式1:[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95%以上。(3-iv)的修饰丝心蛋白与序列号17、序列号11、序列号14或序列号15所示的氨基酸序列具有90%以上的序列一致性,并且从n末端侧向c末端侧依次比较相邻的2个[(a)n基序-rep]单元的rep的氨基酸残基数,将氨基酸残基数少的rep的氨基酸残基数设为1时,并且将另一个rep的氨基酸残基数的比为1.8~11.3的相邻的2个[(a)n基序-rep]单元的氨基酸残基数相加而得到的合计值的最大值设为x、将结构域序列的氨基酸残基总数设为y时,x/y优选为64.2%以上。第3修饰丝心蛋白可以含有用于将重组蛋白生产系统所生产的蛋白质释放到宿主外部的分泌信号。分泌信号的序列可以根据宿主的种类来进行适当设定。将降低甘氨酸残基的含量及(a)n基序的含量的修饰丝心蛋白(第4修饰丝心蛋白)的结构域序列与天然来源的蛛丝类丝心蛋白相比,其除了降低(a)n基序的含量之外,还具有降低甘氨酸残基的含量的氨基酸序列。第4修饰丝心蛋白的结构域序列与天然来源的蛛丝类丝心蛋白相比,其除了至少一个或多个(a)n基序缺失之外,还可以具有相当于至少rep中的一个或多个甘氨酸残基被其他氨基酸残基置换的氨基酸序列。即,第4修饰丝心蛋白为兼具上述降低甘氨酸残基的含量的修饰丝心蛋白(第2修饰丝心蛋白)和降低(a)n基序的含量的修饰丝心蛋白(第3修饰丝心蛋白)的特征的修饰丝心蛋白。具体的实施方式等如第2修饰丝心蛋白及第3修饰丝心蛋白中所说明的那样。作为第4修饰丝心蛋白的更具体的例子,可以列举出包括与(4-i)序列号7、序列号8、序列号9、序列号11、序列号14、序列号15、序列号50、序列号51、序列号52、序列号53、序列号54或序列号57所示的氨基酸序列、或(4-ii)序列号7、序列号8、序列号9、序列号11、序列号14、序列号15、序列号50、序列号51、序列号52、序列号53、序列号54或序列号57所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列的修饰丝心蛋白。序列号7、序列号8、序列号9、序列号11、序列号14、序列号15、序列号50、序列号51、序列号52、序列号53、序列号54或序列号57所示的包含氨基酸序列的修饰丝心蛋白的具体的实施方式如上所述。具有局部包含疏水性指标大的区域的结构域序列的修饰丝心蛋白(第5修饰丝心蛋白)的结构域序列与天然来源的蛛丝类丝心蛋白相比,其可以具有相当于rep中的一个或多个氨基酸残基被置换为疏水性指标大的氨基酸残基及/或在rep中插入了一个或多个疏水性指标大的氨基酸残基的、且局部包含疏水性指标大的区域的氨基酸序列。局部疏水性指标大的区域优选由连续的2~4个氨基酸残基构成。上述疏水性指标大的氨基酸残基更优选为选自异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)、苯丙氨酸(f)、半胱氨酸(c)、蛋氨酸(m)及丙氨酸(a)中的氨基酸残基。第5修饰丝心蛋白与天然来源的蛛丝类丝心蛋白相比,其除了相当于将rep中的一个或多个氨基酸残基置换为疏水性指标大的氨基酸残基及/或在rep中插入一个或多个疏水性指标大的氨基酸残基的修饰之外,进一步与天然来源的蛛丝类丝心蛋白相比,还可以进行相当于与置换、缺失、插入及/或添加一个或多个氨基酸残基的氨基酸序列的修饰。例如可以通过从克隆出的天然来源的蛛丝类丝心蛋白的基因序列中将rep中的一个或多个亲水性氨基酸残基(例如疏水性指标为负的氨基酸残基)置换为疏水性氨基酸残基(例如疏水性指标为正的氨基酸残基)、及/或在rep中插入一个或多个疏水性氨基酸残基,从而得到第5修饰丝心蛋白。此外,例如也可以通过设计出相当于从天然来源的蛛丝类丝心蛋白的氨基酸序列中,将rep中的一个或多个亲水性氨基酸残基置换为疏水性氨基酸残基、及/或在rep中插入一个或多个疏水性氨基酸残基的氨基酸序列,并且对编码所设计的氨基酸序列的核酸进行化学合成后得到。在任何情况下,除了相当于从天然来源的蛛丝类丝心蛋白的氨基酸序列中将rep中的一个或多个亲水性氨基酸残基置换为疏水性氨基酸残基、及/或在rep中插入一个或多个疏水性氨基酸残基的修饰之外,还可以进一步进行与置换、缺失、插入及/或添加一个或多个氨基酸残基相当的氨基酸序列的修饰。第5修饰丝心蛋白包含式1:[(a)n基序-rep]m所示的结构域序列,并且具有下述氨基酸序列:从上述结构域序列中除去自位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列后得到的序列所含的所有rep中,将连续的4个氨基酸残基的疏水性指标的平均值为2.6以上的区域所含的氨基酸残基的总数设为p、将从上述结构域序列中除去自位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列后得到的序列所含的氨基酸残基的总数设为q时,p/q为6.2%以上。关于氨基酸残基的疏水性指标,使用公知的指标(hydropathyindex:kytej,&doolittler(1982)”asimplemethodfordisplayingthehydropathiccharacterofaprotein”,j.mol.biol.,157,pp.105-132)。具体而言,各氨基酸的疏水性指标(亲水指数,以下也记为"hi")。)如下述表1所示。[表1]氨基酸hi氨基酸hi异亮氨酸(ile)4.5色氨酸(trp)-0.9缬氨酸(val)4.2酪氨酸(tyr)-1.3亮氨酸(leu)3.8脯氨酸(pro)-1.6苯丙氨酸(phe)2.8组氨酸(his)-3.2半胱氨酸(cys)2.5天冬酰胺(asn)-3.5蛋氨酸(met)1.9天冬氨酸(asp)-3.5丙氨酸(ala)1.8谷氨酰胺(gln)-3.5甘氨酸(gly)-0.4谷氨酸(glu)-3.5苏氨酸(thr)-0.7赖氨酸(lys)-3.9丝氨酸(ser)-0.8精氨酸(arg)-4.5对p/q的计算方法进一步进行详细说明。在计算中,使用从式1:[(a)n基序-rep]m所示的结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列(以下称为"序列a")。首先,在序列a所包含的所有rep中,计算连续的4个氨基酸残基的疏水性指标的平均值。疏水性指标的平均值是通过将连续的4个氨基酸残基中所含有的各氨基酸残基的hi的总和除以4(氨基酸残基数)而求出的。疏水性指标的平均值是针对所有连续的4个氨基酸残基而求出的(各氨基酸残基用于1~4次平均值的计算)。接下来,确定连续的4个氨基酸残基的疏水性指标的平均值为2.6以上的区域。即使某个氨基酸残基属于多个“疏水性指标的平均值为2.6以上的连续的4个氨基酸残基”的情况下,也会作为一个氨基酸残基包含在区域中。而且,该区域中所含的氨基酸残基的总数为p。此外,序列a中所含的氨基酸残基的总数为q。例如,当提取到20处“疏水性指标的平均值为2.6以上的连续的4个氨基酸残基”时(没有重复),在连续的4个氨基酸残基的疏水性指标的平均值为2.6以上的区域中含有20处连续的4个氨基酸残基(没有重复),p为20×4=80。此外,例如,在2处“疏水性指标的平均值为2.6以上的连续的4个氨基酸残基”仅有一个氨基酸残基重复存在的情况下,在连续的4个氨基酸残基的疏水性指标的平均值为2.6以上的区域中,含有7个氨基酸残基(p=2×4-1=7,“-1”为重复部分的扣除)。例如,在图2所示的结构域序列的情况下,“疏水性指标的平均值为2.6以上的连续的4个氨基酸残基”不重复且存在7个,因此p为7×4=28。此外,例如当为图2所示的结构域序列时,q为4+50+4+40+4+10+4+20+4+30=170(不包含位于c末端侧最后的(a)n基序)。然后,通过将p除以q,可以计算出p/q(%)。在图2的情况下,28/170=16.47%。在第5修饰丝心蛋白中,p/q优选为6.2%以上,更优选为7%以上,进一步优选为10%以上,更进一步优选为20%以上,进一步还优选为30%以上。p/q的上限并没有特别限制,例如可以为45%以下。例如,对于克隆出的天然来源的蛛丝类丝心蛋白的氨基酸序列,通过将rep中的一个或多个亲水性氨基酸残基(例如疏水性指标为负的氨基酸残基)置换为疏水性氨基酸残基(例如疏水性指标为正的氨基酸残基)、及/或在rep中插入一个或多个疏水性氨基酸残基,以使其满足上述p/q的条件,并且通过将其修饰成局部含有疏水性指标大的区域的氨基酸序列,从而得到第5修饰丝心蛋白。此外,例如,也可以通过根据天然来源的蛛丝类丝心蛋白的氨基酸序列设计满足上述p/q的条件的氨基酸序列,并通过对编码所设计的氨基酸序列的核酸进行化学合成后得到。在任何情况下,与天然来源的蛛丝类丝心蛋白相比,除了进行相当于rep中的一个或多个氨基酸残基被置换为疏水性指标大的氨基酸残基、及/或在rep中插入一个或多个疏水性指标大的氨基酸残基的修饰之外,还可以进一步进行相当于置换、缺失、插入及/或添加一个或多个氨基酸残基的修饰。作为疏水性指标大的氨基酸残基,并没有特别限制,优选为异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)、苯丙氨酸(f)、半胱氨酸(c)、蛋氨酸(m)及丙氨酸(a),更优选为缬氨酸(v)、亮氨酸(l)及异亮氨酸(i)。作为第5修饰丝心蛋白的具体例子,可以列举出包括与(5-i)序列号19、序列号20或序列号21所示的氨基酸序列、或者(5-ii)序列号19、序列号20或序列号21所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列的修饰丝心蛋白。对(5-i)的修饰丝心蛋白进行说明。序列号22所示的氨基酸序列通过使天然来源的蛛丝类丝心蛋白的(a)n基序中的丙氨酸残基连续的氨基酸序列发生缺失,从而使得丙氨酸残基连续的个数变为5。序列号19所示的氨基酸序列相对于序列号22所示的氨基酸序列,每隔一个rep插入2处分别由3个氨基酸残基构成的氨基酸序列(vli),并且使c末端侧的部分氨基酸发生缺失以使得其与序列号22所示的氨基酸序列的分子量大致相同。序列号23所示的氨基酸序列相对于序列号22所示的氨基酸序列,各个(a)n基序的c末端侧插入2个丙氨酸残基,进一步将部分谷氨酰胺(q)残基置换为丝氨酸(s)残基、并且使c末端侧的部分氨基酸缺失以使得其与序列号22所示的氨基酸序列的分子量几乎相同。序列号20所示的氨基酸序列相对于序列号23所示的氨基酸序列,每隔一个rep插入一处分别由3个氨基酸残基构成的氨基酸序列(vli)。序列号21所示的氨基酸序列相对于序列号23所示的氨基酸序列,每隔一个rep插入2处分别由3个氨基酸残基构成的氨基酸序列(vli)。(5-i)的修饰丝心蛋白可以由序列号19、序列号20或序列号21所示的氨基酸序列构成。(5-ii)的修饰丝心蛋白包括与序列号19、序列号20或序列号21所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列。(5-ii)的修饰丝心蛋白也为包含式1:[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95%以上。(5-ii)的修饰丝心蛋白与序列号19、序列号20或序列号21所示的氨基酸序列具有90%以上的序列一致性,并且优选地,从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列所含的所有rep中,将连续的4个氨基酸残基的疏水性指标的平均值为2.6以上的区域所含的氨基酸残基的总数设为p、将从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列所含的氨基酸残基的总数设为q时,p/q为6.2%以上。第5修饰丝心蛋白可以在n末端及c末端中的任意一端或两端包含标签序列。作为含有标签序列的第5修饰丝心蛋白的更具体的例子,可以列举出包括与(5-iii)序列号24、序列号25或序列号26所示的氨基酸序列、或(5-iv)序列号24、序列号25或序列号26所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列的修饰丝心蛋白。序列号24、序列号25或序列号26所示的氨基酸序列分别在序列号19、序列号20或序列号21所示的氨基酸序列的n末端添加序列号12所示的氨基酸序列(包含his标签序列及铰链序列)。(5-iii)的修饰丝心蛋白可以由序列号24、序列号25或序列号26所示的氨基酸序列构成。(5-iv)的修饰丝心蛋白包括与序列号24、序列号25或序列号26所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列。(5-iv)的修饰丝心蛋白也为包含式1:[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95%以上。(5-iv)的修饰丝心蛋白与序列号24、序列号25或序列号26所示的氨基酸序列具有90%以上的序列一致性,并且优选地,从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列所含的所有rep中,将连续的4个氨基酸残基的疏水性指标的平均值为2.6以上的区域所含的氨基酸残基的总数设为p、将从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列所含的氨基酸残基的总数设为q时,p/q为6.2%以上。第5修饰丝心蛋白可以含有用于将重组蛋白生产系统所生产的蛋白质释放到宿主外部的分泌信号。分泌信号的序列可以根据宿主的种类来进行适当设定。具有降低谷氨酰胺残基的含量的结构域序列的修饰丝心蛋白(第6修饰丝心蛋白)与天然来源的蛛丝类丝心蛋白相比,具有降低谷氨酰胺残基的含量的氨基酸序列。第6修饰丝心蛋白优选在rep的氨基酸序列中包含选自ggx基序及gpgxx基序中的至少1种基序。第6修饰丝心蛋白在rep中包括gpgxx基序时,gpgxx基序含有率通常为1%以上,也可以为5%以上,优选为10%以上。gpgxx基序含有率的上限并没有特别限制,可以为50%以下,也可以为30%以下。在本说明书中,“gpgxx基序含有率”是通过以下方法计算出的值。在包含式1:[(a)n基序-rep]m或式2:[(a)n基序-rep]m-(a)n基序所示的结构域序列的蛛丝类丝心蛋白中,在从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列所含的所有rep中,当将该区域所含的gpgxx基序的个数的总数乘以3而得到的数(即,相当于gpgxx基序中的g及p的总数)设为s,并且将从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列且除去(a)n基序后得到的所有rep的氨基酸残基的总数设为t时,以s/t来计算gpgxx基序含有率。在gpgxx基序含有率的计算中,将“从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列”作为对象是为了排除下述影响:“位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列”(相当于rep的序列)中有时包含与蛛丝类丝心蛋白的特征性序列相关性低的序列,在m较小的情况下(也就是说,结构域序列短的情况下)会影响gpgxx基序含有率的计算结果。另外,在“gpgxx基序”位于rep的c末端的情况下,即使“xx”例如为“aa”时,也作为“gpgxx基序”来进行处理。图3是表示蛛丝类丝心蛋白的结构域序列的示意图。参照图3来具体说明gpgxx基序含有率的计算方法。首先,在图3所示的蛛丝类丝心蛋白的结构域序列(“[(a)n基序-rep]m-(a)n基序”类型)中,所有rep都包含在“从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列”(图3中“区域a”所示的序列)中,因此用于计算s的gpgxx基序的个数为7,s为7×3=21。同样地,由于所有rep都包含在“从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列”(图3中“区域a”所示的序列)中,因此从该序列中进一步除去(a)n基序后得到的所有rep的氨基酸残基的总数t为50+40+10+20+30=150。接下来,通过将s除以t,可以计算出s/t(%),在图3的丝心蛋白的情况下,为21/150=14.0%。在第6修饰丝心蛋白中,谷氨酰胺残基含有率优选为9%以下,更优选为7%以下,进一步优选为4%以下,特别优选为0%。在本说明书中,“谷氨酰胺残基含有率”是通过以下方法计算出的值。在包含式1:[(a)n基序-rep]m或式2:[(a)n基序-rep]m-(a)n基序所示的结构域序列的蛛丝类丝心蛋白中,在从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列(相当于图3的“区域a”的序列)所含的所有rep中,当将该区域所含的谷氨酰胺残基的总数设为u,并且将从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列且除去(a)n基序后得到的所有rep的氨基酸残基的总数设为t时,以u/t来计算谷氨酰胺残基含有率。在谷氨酰胺残基含有率的计算中,以“从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列”为对象的理由与上述的理由相同。第6修饰丝心蛋白的结构域序列与天然来源的蛛丝类丝心蛋白相比,可以具有相当于使rep中的一个或多个谷氨酰胺残基发生缺失或置换为其他氨基酸残基的氨基酸序列。“其他氨基酸残基”只要是谷氨酰胺残基以外的氨基酸残基即可,优选为疏水性指标大于谷氨酰胺残基的氨基酸残基。氨基酸残基的疏水性指标如表1所示。如表1所示,作为疏水性指标大于谷氨酰胺残基的氨基酸残基,可以列举出选自异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)、苯丙氨酸(f)、半胱氨酸(c)、蛋氨酸(m)、丙氨酸(a)、甘氨酸(g)、苏氨酸(t)、丝氨酸(s)、色氨酸(w)、酪氨酸(y)、脯氨酸(p)及组氨酸(h)中的氨基酸残基。其中,更优选为选自异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)、苯丙氨酸(f)、半胱氨酸(c)、蛋氨酸(m)及丙氨酸(a)中的氨基酸残基,进一步优选为选自异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)及苯丙氨酸(f)中的氨基酸残基。第6修饰丝心蛋白中的rep的疏水性程度优选为-0.8以上,更优选为-0.7以上,进一步优选为0以上,更进一步优选为0.3以上,特别优选为0.4以上。rep的上限并没有特别限制,可以为1.0以下,也可以为0.7以下。在本说明书中,“rep的疏水性程度”为通过以下方法而计算出的值。在包含式1:[(a)n基序-rep]m或式2:[(a)n基序-rep]m-(a)n基序所示的结构域序列的蛛丝类丝心蛋白中,在从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列(相当于图3的“区域a”的序列)所含的所有rep中,当将该区域的各氨基酸残基的疏水性指标的总和设为v,并且将从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列且除去(a)n基序后得到的所有rep的氨基酸残基的总数设为t时,以v/t来计算rep的疏水性程度。在rep的疏水性程度的计算中,以“从结构域序列中除去自位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列后得到的序列”为对象的理由与上述的理由相同。第6修饰丝心蛋白的结构域序列与天然来源的蛛丝类丝心蛋白相比,其除了相当于缺失了rep中的一个或多个谷氨酰胺残基、及/或将rep中的一个或多个谷氨酰胺残基置换为其他氨基酸残基的的修饰之外,还可以进一步进行相当于置换、缺失、插入及/或添加一个或多个氨基酸残基的氨基酸序列的修饰。例如可以通过在克隆出的天然来源的蛛丝类丝心蛋白的基因序列中使rep中的一个或多个谷氨酰胺残基发生缺失、及/或将rep中的一个或多个谷氨酰胺残基置换为其他氨基酸残基,从而得到第6修饰丝心蛋白。此外,例如也可以通过设计出相当于在天然来源的蛛丝类丝心蛋白的氨基酸序列中,使rep中的一个或多个谷氨酰胺残基发生缺失、及/或将rep中的一个或多个谷氨酰胺残基置换为其他氨基酸残基的氨基酸序列,并且对编码所设计的氨基酸序列的核酸进行化学合成后得到。作为第6修饰丝心蛋白的更具体的例子,可以列举出包括(6-i)序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号33或序列号43所示的氨基酸序列的修饰丝心蛋白,或者包括与(6-ii)序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号33或序列号43所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列的修饰丝心蛋白。对(6-i)的修饰丝心蛋白进行说明。序列号7所示的氨基酸序列(met-prt410)根据作为天然来源的丝心蛋白的nephilaclavipes(genbank登录号:p46804.1、gi:1174415)的碱基序列及氨基酸序列,对(a)n基序中的丙氨酸残基连续而成的氨基酸序列进行使丙氨酸残基连续数为5个等的用于提高生产率的氨基酸修饰。另一方面,met-prt410未进行谷氨酰胺残基(q)的修饰,因此谷氨酰胺残基含有率与天然来源的丝心蛋白的谷氨酰胺残基含有率相同。序列号27所示的氨基酸序列(m_prt888)是将met-prt410(序列号7)中的qq全部置换为vl而得到的氨基酸序列。序列号28所示的氨基酸序列(m_prt965)是将met-prt410(序列号7)中的qq全部置换为ts、并且将其余的q置换为a而得到的氨基酸序列。序列号29所示的氨基酸序列(m_prt889)是将met-prt410(序列号7)中的qq全部置换为vl、并且将其余的q置换为i而得到的氨基酸序列。序列号30所示的氨基酸序列(m_prt916)是将met-prt410(序列号7)中的qq全部置换为vi、并且将其余的q置换为l而得到的氨基酸序列。序列号31所示的氨基酸序列(m_prt918)是将met-prt410(序列号7)中的qq全部置换为vf、并且将其余的q置换为i而得到的氨基酸序列。序列号34所示的氨基酸序列(m_prt525)相对于met-prt410(序列号7),在丙氨酸残基连续而成的区域(a5)中插入2个丙氨酸残基、使c末端侧的结构域序列缺失2个以使得其与met-prt410的分子量几乎相同、并且将13处的谷氨酰胺残基(q)置换为丝氨酸残基(s)或脯氨酸残基(p)而得到的氨基酸序列。序列号32所示的氨基酸序列(m_prt699)是将m_prt525(序列号34)中的qq全部置换为vl而得到的氨基酸序列。序列号33所示的氨基酸序列(m_prt698)是将m_prt525(序列号34)中的qq全部置换为vl、并且将其余的q置换为i而得到的氨基酸序列。序列号43所示的氨基酸序列(met-prt966)是将序列号9所示的氨基酸序列(在c末端添加序列号42所示的氨基酸序列之前的氨基酸序列)中的qq全部置换为vf,并且将其余的q置换为i而得到的氨基酸序列。序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号33及序列号43所示的氨基酸序列的谷氨酰胺残基含有率均为9%以下(表2)。[表2](6-i)的修饰丝心蛋白可以由序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号33或序列号43所示的氨基酸序列构成。((6-ii)的修饰丝心蛋白包括与序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号33或序列号43所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列。(6-ii)的修饰丝心蛋白也是包括式1:[(a)n基序-rep]m、或式2:[(a)n基序-rep]m-(a)n基序所示的结构域序列的蛋白质。上述序列一致性优选为95%以上。(6-ii)的修饰丝心蛋白的谷氨酰胺残基含有率优选为9%以下。此外,(6-ii)的修饰丝心蛋白的gpgxx基序含有率优选为10%以上。第6修饰丝心蛋白可以在n末端及c末端中的任意一端或两端包含标签序列。由此,可以实现修饰丝心蛋白的分离、固定、检测及可视化等。作为含有标签序列的第6修饰丝心蛋白的更具体的例子,可以列举出包括(6-iii)序列号35、序列号36、序列号37、序列号38、序列号39、序列号40、序列号41、序列号44、序列号55或序列号56所示的氨基酸序列的修饰丝心蛋白,或者包括与(6-iv)序列号35、序列号36、序列号37、序列号38、序列号39、序列号40、序列号41、序列号44、序列号55或序列号56所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列的修饰丝心蛋白。序列号35、序列号36、序列号37、序列号38、序列号39、序列号40、序列号41及序列号44所示的氨基酸序列分别在序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号33及序列号43所示的氨基酸序列的n末端添加序列号12所示的氨基酸序列(包含his标签序列及铰链序列)。由于仅在n末端添加了标签序列,因此谷氨酰胺残基含有率没有变化,序列号35、序列号36、序列号37、序列号38、序列号39、序列号40、序列号41及序列号44所示的氨基酸序列的谷氨酰胺残基含有率均为9%以下(表3)。在序列号55所示的氨基酸序列(prt1107)中,将序列号31所示的氨基酸序列(met-prt918)的丝氨酸残基(s)置换为丙氨酸残基(a)、缬氨酸残基(v)、亮氨酸残基(l)或异亮氨酸残基(i),并进一步在n末端添加标签序列。在序列号56所示的氨基酸序列(prt1083)中,将序列号31所示的氨基酸序列(met-prt918)的脯氨酸残基(p)置换为苏氨酸残基(t)或亮氨酸残基(l),并进一步在n末端添加标签序列。[表3](6-iii)的修饰丝心蛋白可以由序列号35、序列号36、序列号37、序列号38、序列号39、序列号40、序列号41、序列号44、序列号55或序列号56所示的氨基酸序列构成。(6-iv)的修饰丝心蛋白包括与序列号35、序列号36、序列号37、序列号38、序列号39、序列号40、序列号41、序列号44、序列号55或序列号56所示的氨基酸序列具有90%以上的序列一致性的氨基酸序列。(6-iv)的修饰丝心蛋白也是包括式1:[(a)n基序-rep]m、或式2:[(a)n基序-rep]m-(a)n基序所示的结构域序列的蛋白质。上述序列一致性优选为95%以上。(6-iv)的修饰丝心蛋白的谷氨酰胺残基含有率优选为9%以下。此外,(6-iv)的修饰丝心蛋白的gpgxx基序含有率优选为10%以上。第6修饰丝心蛋白可以含有用于将重组蛋白生产系统所生产的蛋白质释放到宿主外部的分泌信号。分泌信号的序列可以根据宿主的种类来进行适当设定。修饰丝心蛋白可以为兼具第1修饰丝心蛋白、第2修饰丝心蛋白、第3修饰丝心蛋白、第4修饰丝心蛋白、第5修饰丝心蛋白及第6修饰丝心蛋白所具有的特征中的至少2种以上特征的修饰丝心蛋白。蜘蛛丝蛋白可以为亲水性蜘蛛丝蛋白,也可以为疏水性蜘蛛丝蛋白。所谓疏水性蜘蛛丝蛋白,是指求出构成蜘蛛丝蛋白的所有氨基酸残基的疏水性指标(hi)的总和,然后将该总和除以氨基酸残基总数后得到的值(平均hi)超过-0.8的蜘蛛丝蛋白,更优选平均hi为-0.6以上的蛋白质,更优选平均hi为-0.4以上的蛋白质,进一步优选平均hi为-0.2以上的蛋白质,特别优选平均hi为0以上的蜘蛛丝蛋白。疏水性指标如表1所示。此外,亲水性蜘蛛丝蛋白是指上述平均hi为-0.8以下的蜘蛛丝蛋白。本实施方式所涉及的蛋白质的平均疏水性指标(hi)优选为-1.3以上,或优选为-1.0以上,或优选为-0.8以上,或优选为大于-0.8,或优选为-0.7以上,或优选为-0.6以上,更优选为-0.5以上,或优选为-0.4以上,或优选为-0.3以上,或优选为-0.2以上,或优选为-0.1以上,更优选为0以上,或更优选为0.1以上,或更优选为0.2以上,进一步优选为0.3以上,特别优选为0.4以上。序列号11、序列号15、序列号35、序列号36、序列号37、序列号38、序列号39、序列号40及序列号41所示的氨基酸序列的hi如表4所示。在计算各氨基酸序列的hi时,除去与修饰丝心蛋白无关的序列(即,相当于序列号12所示的氨基酸序列的序列)后进行计算。[表4]氨基酸序列疏水性程度序列号11所示的氨基酸序列-0.8序列号15所示的氨基酸序列-0.8序列号35所示的氨基酸序列0.07序列号36所示的氨基酸序列-0.16序列号37所示的氨基酸序列0.55序列号38所示的氨基酸序列0.54序列号39所示的氨基酸序列0.49序列号40所示的氨基酸序列0.21序列号41所示的氨基酸序列0.48序列号45所示的氨基酸序列-0.74序列号47所示的氨基酸序列-1.2序列号48所示的氨基酸序列0.47序列号49所示的氨基酸序列-0.531作为疏水性蜘蛛丝蛋白,例如,可以列举出上述第1修饰丝心蛋白的序列、第2修饰丝心蛋白的序列、第3修饰丝心蛋白的序列、第5修饰丝心蛋白的序列及第6修饰丝心蛋白的序列。作为疏水性蜘蛛丝蛋白的更具体的例子,可以列举出包含序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号33或序列号43所示的氨基酸序列、以及序列号35、序列号37、序列号38、序列号39、序列号40、序列号41或序列号44所示的氨基酸序列的蜘蛛丝蛋白。作为亲水性蜘蛛丝蛋白,例如可以列举出上述的第4修饰丝心蛋白的序列。作为亲水性蜘蛛丝蛋白的更具体的例子,可以列举出包括序列号4所示的氨基酸序列,序列号6、序列号7、序列号8或序列号9所示的氨基酸序列,序列号13、序列号11、序列号14或序列号15所示的氨基酸序列,序列号18、序列号7、序列号8或序列号9所示的氨基酸序列,序列号17、序列号11、序列号14或序列号15所示的氨基酸序列,序列号19、序列号20、序列号21或序列号47所示的氨基酸序列的蜘蛛丝蛋白。上述的蜘蛛丝蛋白可以单独使用1种,或者组合使用2种以上。例如,通过对具有编码该蜘蛛丝蛋白的核酸序列和以可工作的方式连接于该核酸序列的一个或多个调控序列的表达载体进行转化的宿主来表达该核酸,从而可以生产蜘蛛丝蛋白。编码蜘蛛丝蛋白的核酸的制备方法并没有特别限制。例如,可以通过利用编码天然的蜘蛛丝蛋白的基因,并通过聚合酶链式反应(pcr)进行扩增、克隆的方法,或进行化学合成的方法来制造该核酸。核酸的化学合成方法也没有特别限制,例如,可以通过将基于由ncbi的网络数据库等获得的蜘蛛丝蛋白的氨基酸序列信息、并且用aktaoligopilotplus10/100(gehealthcare·japan株式会社)等自动合成的寡核苷酸利用pcr等进行连接的方法来化学合成基因。此时,为了容易地进行蜘蛛丝蛋白的纯化及/或确认,可以对编码在n末端添加了由起始密码子及his10标签构成的氨基酸序列的氨基酸序列所构成的蜘蛛丝蛋白的核酸进行合成。调控序列为控制宿主中的重组蛋白的表达的序列(例如启动子、增强子、核糖体结合序列、转录终止序列等),并且可以根据宿主的种类进行适当选择。作为启动子,也可以使用在宿主细胞中发挥功能,可表达诱导作为目标的蜘蛛丝蛋白的诱导性启动子。诱导性启动子为可以通过诱导物质(表达诱导剂)的存在、阻遏分子的不存在或者温度、渗透压或ph值的上升或下降等物理因素来控制转录的启动子。表达载体的种类可以根据宿主的种类来适当地选择质粒载体、病毒载体、柯斯质粒载体、福斯质粒载体、人工染色体载体等。作为表达载体,优选使用在宿主细胞中能够自主复制、或者能够整合到宿主的染色体中且在能够转录编码蜘蛛丝蛋白的核酸的位置处包含启动子的载体。作为宿主,可以适宜地使用原核生物以及酵母、丝状真菌、昆虫细胞、动物细胞及植物细胞等真核生物中的任意一个。在使用细菌等原核生物作为宿主的情况下,表达载体优选为能够在原核生物中自主复制且同时包含启动子、核糖体结合序列、编码蜘蛛丝蛋白的核酸及转录终止序列的载体。也可以含有控制启动子的基因。作为原核生物,可以列举出属于埃希氏菌属、短小芽孢杆菌属、沙雷氏菌属、芽孢杆菌属、微杆菌属、短杆菌属、棒杆菌属及假单胞菌属等的微生物。作为属于埃希氏菌属的微生物,例如,可以列举出大肠杆菌等。作为属于短小芽孢杆菌属的微生物,例如,可以列举出土壤短小芽孢杆菌等。作为属于沙雷氏菌属的微生物,例如,可以列举出液化沙雷氏菌等。作为属于芽孢杆菌属的微生物,例如,可以列举出枯草芽孢杆菌等。作为属于微杆菌属的微生物,例如,可以列举出嗜氨微杆菌等。作为属于短杆菌属的微生物,例如,可以列举出叉开短杆菌等。作为属于棒杆菌属的微生物,例如,可以列举出产氨棒杆菌等。作为属于假单胞菌(pseudomonas)属的微生物,例如,可以列举出恶臭假单胞菌等。在以原核生物作为宿主的情况下,作为导入编码蜘蛛丝蛋白的核酸的载体,例如,可以列举出pbtrp2(勃林格殷格翰企业制)、pgex(pharmacia企业制)、puc18、pbluescriptii、psupex、pet22b、pcold、pub110、pnco2(日本特开2002-238569号公报)等。作为真核生物宿主,例如,可以列举出酵母及丝状真菌(霉菌等)。作为酵母,例如,可以列举出属于酵母属、毕赤酵母属、裂殖酵母属等的酵母。作为丝状真菌,例如,可以列举出属于曲霉属、青霉属、木霉(trichoderma)属等的丝状真菌。在以真核生物作为宿主的情况下,作为导入编码蜘蛛丝蛋白的核酸的载体,例如,可以列举出yep13(atcc37115)、yep24(atcc37051)等。作为向上述宿主细胞中导入表达载体的方法,只要是向上述宿主细胞中导入dna的方法都可以使用。例如,可以列举出使用钙离子的方法〔proc.natl.acad.sci.usa,69,2110(1972)〕、电穿孔法、原生质球法、原生质体法、乙酸锂法、感受态细胞法等。作为基于利用表达载体进行转化后的宿主的核酸表达方法,除了直接表达以外,还可以依据分子克隆第2版中记载的方法等进行分泌生产、融合蛋白表达等。例如,可以将转化后的宿主在培养用培养基中培养,并通过使该蜘蛛丝蛋白在培养用培养基中生成并蓄积,并且从该培养用培养基中收集,从而可以制备蜘蛛丝蛋白。在培养用培养基中培养转化后的宿主的方法可以按照在宿主的培养中通常使用的方法来进行。在宿主为大肠杆菌等原核生物或酵母等真核生物的情况下,作为培养用培养基,只要是含有该宿主可同化的碳源、氮源及无机盐类等、并且能够高效地进行该宿主的培养的培养基,则可以使用天然培养基、合成培养基中的任意一种。作为碳源,只要是该宿主可同化的物质即可,例如,可以使用葡萄糖、果糖、蔗糖以及含有这些糖的糖蜜、淀粉及淀粉水解物等碳水化合物、乙酸及丙酸等有机酸、以及乙醇及丙醇等醇类。作为氮源,例如,可以使用氨、氯化铵、硫酸铵、乙酸铵及磷酸铵等无机酸或有机酸的铵盐、其它含氮化合物、以及蛋白胨、肉提取物、酵母提取物、玉米浆、酪蛋白水解物、豆粕及豆粕水解物、各种发酵菌体及其消化产物。作为无机盐类,例如,可以使用磷酸氢钾、磷酸氢二钾、磷酸镁、硫酸镁、氯化钠、硫酸亚铁、硫酸锰、硫酸铜及碳酸钙。大肠杆菌等原核生物或酵母等真核生物的培养例如可以在振荡培养或深部通气搅拌培养等需氧条件下进行。培养温度例如为15~40℃。培养时间通常为16小时~7天。培养中的培养用培养基的ph优选保持在3.0~9.0之间。培养用培养基的ph的调整可以使用无机酸、有机酸、碱溶液、尿素、碳酸钙及氨等进行。此外,在培养中,可以根据需要在培养用培养基中添加氨苄青霉素及四环素等抗生素。当对通过使用诱导型启动子以作为启动子的表达载体进行转化后的微生物进行培养时,可以根据需要在培养基中添加诱导剂。例如,在对通过使用lac启动子的表达载体进行转化后的微生物进行培养时,可以在培养基中添加异丙基-β-d-硫代半乳糖吡喃糖苷等;在对通过使用trp启动子的表达载体进行转化后的微生物进行培养时,可以在培养基中添加吲哚丙烯酸等。由转化后的宿主生产的蜘蛛丝蛋白可以通过通常用于蛋白质的分离纯化的方法进行分离及纯化。例如,在蜘蛛丝蛋白以溶解状态在细胞内表达的情况下,在培养结束后,通过离心分离回收宿主细胞,悬浮于水系缓冲液中后,利用超声波破碎机、弗氏细胞压碎器、manton-gaulin高压匀浆器及戴诺研磨机等将宿主细胞破碎,从而得到无细胞提取液。从通过对该无细胞提取液进行离心分离而得到的上清液中,单独或组合使用蛋白质的分离纯化中通常使用的方法、即溶剂提取法、利用硫酸铵等的盐析法、脱盐法、利用有机溶剂的沉淀法、使用二乙氨基乙基(deae)-琼脂糖、diaionhpa-75(三菱化成企业制)等树脂的阴离子交换层析法、使用s-sepharoseff(pharmacia企业制)等树脂的阳离子交换层析法、使用丁基琼脂糖、苯基琼脂糖等树脂的疏水性层析法、使用分子筛的凝胶过滤法、亲及层析法、色谱聚焦法、等电点电泳等电泳法等方法,能够得到纯化制备品。作为上述层析,优选采用使用了phenyl-toyopearl(东曹)、deae-toyopearl(东曹)、sephadexg-150(pharmaciabiotech)的柱层析。另外,在蜘蛛丝蛋白在细胞内形成不溶体而进行表达的情况下,同样地回收宿主细胞后将其破碎并进行离心分离,由此以沉淀分级的形式回收蜘蛛丝蛋白的不溶体。回收的蜘蛛丝蛋白的不溶体可以利用蛋白质变性剂进行可溶化。该操作后,通过与上述同样的分离纯化法可以得到蜘蛛丝蛋白的纯化标准品。在蜘蛛丝蛋白分泌到细胞外的情况下,可以从培养上清液中回收蜘蛛丝蛋白。即,通过利用离心分离等方法对培养物进行处理来获得培养上清液,通过使用与上述同样的分离纯化法,能够从该培养上清液中获得纯化标准品。作为来自于胶原的结构蛋白质(胶原蛋白),例如,可以列举出包含式3:[rep3]p所示的结构域序列的结构蛋白质(其中,在式3中,p表示5~300的整数;rep3表示由gly-x-y构成的氨基酸序列;x及y表示除gly以外的任意的氨基酸残基;多个存在的rep3可以是相互相同的氨基酸序列,也可以是不同的氨基酸序列。)。具体而言,可以列举出包含序列号45所示的氨基酸序列的结构蛋白质。序列号45所示的氨基酸序列将序列号46所示的氨基酸序列(标签序列及铰链序列)添加至与从ncbi数据库获得的人四型胶原蛋白的部分序列(ncbi的genbank登录号:caa56335.1,gi:3702452)的重复部分及基序相对应的从第301个残基至第540个残基的氨基酸序列的n末端。此外,作为来自于胶原的结构蛋白质,可以列举出包含序列号59所示的氨基酸序列的结构蛋白质。作为来自于节肢弹性蛋白的结构蛋白质(节肢弹性蛋白),例如,可以列举出包含式4:[rep4]q所示的结构域序列的结构蛋白质(其中,在式4中,q表示4~300的整数。rep4表示由ser-j-j-tyr-gly-u-pro构成的氨基酸序列。j表示任意的氨基酸残基,特别优选为选自由asp、ser及thr构成的组中的氨基酸残基。u表示任意的氨基酸残基,特别优选为选自由pro、ala、thr及ser构成的组中的氨基酸残基。存在的多个rep4可以是彼此相同的氨基酸序列,也可以是彼此不同的氨基酸序列。具体而言,可以列举出包含序列号47所示的氨基酸序列的结构蛋白质。序列号47所示的氨基酸序列将序列号46所示的氨基酸序列(标签序列及铰链序列)添加至用于在节肢弹性蛋白(ncbi的genbank登录号np611157、gl:24654243)的氨基酸序列中将第87个残基的thr置换为ser、且将第95个残基的asn置换为asp后得到的序列的第19个残基至第321个残基的氨基酸序列的n末端。此外,作为来自于节肢弹性蛋白的结构蛋白质,可以列举出包含序列号60所示的氨基酸序列的结构蛋白质。作为来自于弹性蛋白的结构蛋白质(弹性蛋白),例如可以列举出ncbi的genbank登录号aac98395(人)、i47076(羊)、np786966(牛)等具有氨基酸序列的结构蛋白质。具体而言,可以列举出包含序列号48所示的氨基酸序列的结构蛋白质。序列号48所示的氨基酸序列将序列号46所示的氨基酸序列(标签序列及铰链序列)添加至ncbi的genbank登录号aac98395的氨基酸序列的第121个残基至第390个残基的氨基酸序列的n末端。作为来自于角蛋白的结构蛋白质(角蛋白),例如,可以列举出山羊(caprahircus)的i类型角蛋白等。具体而言,可以列举出包含序列号49所示的氨基酸序列(ncbi的genbank登录号acy30466的氨基酸序列)的结构蛋白质。序列号49所示的氨基酸序列将序列号46所示的氨基酸序列(标签序列及铰链序列)添加至ncbi的genbank登录号acy30466的氨基酸序列的n末端。此外,例如,作为来自于角蛋白的结构蛋白质,可以列举出有包含序列号58所示的氨基酸序列的结构蛋白质。序列号58所示的氨基酸序列相对于序列号49的从n末端起的第1~292个氨基酸残基组成的氨基酸序列、以及将亮氨酸或缬氨酸置换成丙氨酸或甘氨酸的氨基酸序列,具有对从n末端起的第1~246个氨基酸残基中的3个氨基酸残基进行置换、以及对插入由gaaaaag(序列号62)构成的氨基酸序列后得到的氨基酸序列进行重复的氨基酸序列。胶原蛋白、节肢弹性蛋白、弹性蛋白及角蛋白可以是亲水性蛋白质,也可以是疏水性蛋白质。所谓疏水性蛋白质,是指求出构成上述蛋白质的所有氨基酸残基的疏水性指标(hi)的总和,然后将该总和除以氨基酸残基总数后得到的值(平均hi)超过-0.8的蛋白质,更优选平均hi为-0.6以上的蛋白质,更优选平均hi为-0.4以上的蛋白质,进一步优选平均hi为-0.2以上的蛋白质,特别优选平均hi为0以上的蛋白质。疏水性指标如表1所示。此外,亲水性蛋白质是指上述平均hi为-0.8以下的蛋白质。作为疏水性胶原蛋白、疏水性节肢弹性蛋白、疏水性弹性蛋白及疏水性角蛋白,例如,可以列举出包含上述序列号45、序列号48或序列号49所示的氨基酸序列的蛋白质。作为亲水性胶原蛋白、亲水性节肢弹性蛋白、亲水性弹性蛋白及亲水性角蛋白,例如,可以列举出包含上述序列号47所示的氨基酸序列的蛋白质。序列号45、序列号47、序列号48及序列号49所示的氨基酸序列的hi如表4所示。当计算各个氨基酸序列的hi时,除去与胶原蛋白、节肢弹性蛋白、弹性蛋白以及角蛋白无关的序列(即,相当于序列号12所示的氨基酸序列的序列)后计算。此外,结构蛋白质包括疏水性蛋白质及在极性溶剂中具有容易发生自凝集倾向的多肽,并且结构蛋白质优选为疏水性蛋白质。结构蛋白质或来自其的结构蛋白质可以单独使用1种,或者组合使用2种以上。通过组合2种以上的结构蛋白质,可以将作为整体的疏水性程度调节为所希翼的值。疏水性程度可以通过上述方法进行计算。(有机溶剂)本实施方式所涉及的纺丝原液的有机溶剂,只要是能够溶解人造蛋白质的有机溶剂,都可以使用。作为有机溶剂,例如,可以列举出六氟异丙醇(hfip)、六氟丙酮(hfa)、二甲基亚砜(dmso)、n,n-二甲基甲酰胺(dmf)、n,n-二甲基乙酰胺(dma)、1,3-二甲基-2-咪唑啉酮(dmi)、n-甲基-2-吡咯烷酮(nmp)、乙腈、n-甲基吗啉n-氧化物(nmo)及甲酸等。这些溶剂可以单独使用1种,或者组合使用2种以上。例如,有机溶剂可以包含选自由甲酸、dmso及hfip构成的组中的至少1种,也可以是选自由甲酸、dmso及hfip构成的组中的至少1种,或者也可以是甲酸。这些有机溶剂也可以含水。当将纺丝原液总量设为100质量%时,本实施方式所涉及的纺丝原液中的蛋白质含量优选为10~40质量%,更优选为10~35质量%,更优选为12~35质量%,还可以优选为15~35质量%,更优选为15~30质量%,进一步优选为20~35质量%,特别优选为20~30质量%。当结构蛋白质的含量为10质量%以上时,在凝固浴中形成的纤维可以进一步降低在凝固浴中产生的伴随流的影响,并且提高生产率。当结构蛋白质的含量为40质量%以下时,可以从纺丝喷丝头更加稳定地喷出纺丝原液,并且提高生产率。(溶解促进剂)本实施方式所涉及的纺丝原液可以进一步含有溶解促进剂。通过含有溶解促进剂,纺丝原液的制备变得容易。溶解促进剂可以是由以下所示的路易斯酸和路易斯碱构成的无机盐。作为路易斯碱,例如,可以列举出卤化物离子等。作为路易斯酸,例如,可以列举出碱金属离子、卤化物碱土金属离子等金属离子等。作为无机盐,例如,可以列举出碱金属卤化物及碱土金属卤化物。作为碱金属卤化物的具体实施例,可以列举出氯化锂、溴化锂等。作为碱土卤化物的具体实施例,可以列举出氯化镁、氯化钙等。溶解促进剂可以单独使用1种,或者组合使用2种以上。这些无机盐可以用作结构蛋白质在甲酸或dmso中的溶解促进剂,特别优选为氯化锂及氯化钙。通过纺丝原液含有溶解促进剂(上述无机盐),结构蛋白质可以高浓度地溶解在纺丝原液中。由此,进一步提高蛋白质纤维的生产效率,并且可以期待提高蛋白质纤维的品质及应力等物理性质。相对于纺丝原液总量,溶解促进剂的含量可以为0.1质量%以上、1质量%以上、2质量%以上、3质量%以上、4质量%以上、7质量%以上、10质量%以上或15质量%以上,还可以为20质量%以下、16质量%以下、12质量%以下或9质量%以下。(各种添加剂)纺丝原液根据需要还可以进一步含有各种添加剂。作为添加剂,例如,可以列举出增塑剂、流平剂、交联剂、结晶成核剂、抗氧化剂、紫外线吸取剂、着色剂、填料及合成树脂。相对于纺丝原液中的蛋白质总量100质量份,添加剂含量可以为50质量份以下。本实施方式所涉及的纺丝原液的粘度可以根据所制备的纤维的用途或纺丝方法等来进行适当设定。例如,在20℃下,可以是60,000~130,000mpa·sec,也可以是65,000~125,000mpa·sec。此外,例如,在35℃下,可以是500~35,000mpa·sec,也可以是1,000~35,000mpa·sec,也可以是3,000~30,000mpa·sec,也可以是500~20,000mpa·sec,也可以是500~15,000mpa·sec,也可以是1,000~15,000mpa·sec,也可以是1,000~12,000mpa·sec,也可以是1,500~12,000mpa·sec,也可以是1,500~10,000mpa·sec,也可以是1,500~8,000mpa·sec等。此外,例如,在40℃下,可以是500~35,000mpa·sec,也可以是1,000~35,000mpa·sec,也可以是5,000~35,000mpa·sec,也可以是10,000~30,000mpa·sec,也可以是12,000~30,000mpa·sec,也可以是12,000~28,000mpa·sec等。此外,例如,在70℃下,可以是1,000~6,000mpa·sec,也可以是1,500~5,000mpa·sec等。纺丝原液的粘度可以使用例如京都电子工业企业制的商品名“ems粘度计”来进行测量。为了促进溶解,可以将纺丝原液搅拌或振荡一段时间。此时,根据需要,纺丝原液可以根据所使用的结构蛋白质及溶剂加热到可溶解的温度。纺液例如可以加热至30℃以上、40℃以上、50℃以上、60℃以上、70℃以上、80℃以上、或90℃以上。从进一步防止人造蛋白质的分解的观点出发,优选为40℃。加热温度的上限例如为溶剂的沸点以下。<凝固液>本实施方式所涉及的凝固液含有水或ph为0.25以上且ph为10.00以下的水溶液。由此,可以提供一种蛋白质纤维的制备方法,其降低了爆炸/火灾等危险性、制造成本以及环境负荷。水溶液可以是盐水溶液、酸水溶液或盐水溶液与酸水溶液的混合溶液,还可以是盐水溶液或盐水溶液与酸水溶液的混合溶液,还可以是盐水溶液。在此,盐水溶液和酸水溶液的混合溶液并不限定于混合了盐水溶液和酸水溶液的溶液,也包括在盐水溶液中混合了酸的溶液、在酸水溶液中混合了盐的溶液、以及在水中溶解了盐和酸的溶液。(酸水溶液)作为酸水溶液,可以列举出羧酸等的水溶液,并且作为羧酸的具体实施例,可以列举出甲酸、乙酸、丙酸、柠檬酸及草酸等。这些溶剂可以单独使用1种,或者混合2种以上作为水溶液使用。例如,酸水溶液还可以是柠檬酸水溶液或甲酸水溶液。(盐水溶液)作为盐水溶液,可以列举出有机盐或无机盐的盐水溶液、以及有机盐及无机盐的混合水溶液等。作为有机盐,例如可以列举出羧酸盐等,并且作为羧酸盐的具体实施例,可以列举出甲酸盐、乙酸盐、丙酸盐、柠檬酸盐及草酸盐等。例如,有机盐还可以是甲酸盐、乙酸盐及柠檬酸盐。作为甲酸盐的具体实施例,例如可以列举出甲酸铵、甲酸钾、甲酸钠、甲酸锂、甲酸镁及甲酸钙等。作为乙酸盐的具体实施例,例如可以列举出乙酸铵、乙酸钾、乙酸钠、乙酸锂、乙酸镁及乙酸钙等。作为丙酸盐的具体实施例,例如可以列举出丙酸铵、丙酸钾、丙酸钠、丙酸锂、丙酸镁及丙酸钙等。作为柠檬酸盐的具体实施例,可以列举出柠檬酸铵、柠檬酸钾、柠檬酸钠、柠檬酸锂、柠檬酸镁及柠檬酸钙等。例如,柠檬酸盐可以包括选自由柠檬酸铵、柠檬酸钾、柠檬酸钠、柠檬酸镁及柠檬酸钙构成的组中的至少1种,还可以包括选自由柠檬酸铵、柠檬酸钾及柠檬酸钠构成的组中的至少1种,还可以包括选自由柠檬酸钾及柠檬酸钠构成的组中的至少1种,还可以是柠檬酸钠。作为草酸盐的具体实施例,可以列举出草酸铵、草酸钾、草酸钠、草酸锂、草酸镁及草酸钙等。作为羧酸盐,更优选为羧酸钠,作为羧酸钠的具体实施例,可以例举出甲酸钠、乙酸钠、丙酸钠及草酸钠等。作为无机盐的具体实施例,可以列举出正盐、酸性盐及碱性盐。作为正盐的具体实施例,可以列举出硫酸盐、氯化物、硝酸盐、碘化物盐、硫氰酸盐以及碳酸盐等。作为硫酸盐的具体实施例,例如可以列举出硫酸铵、硫酸钾、硫酸钠、硫酸锂、硫酸镁及硫酸钙等。例如,硫酸盐可以包括选自由硫酸铵、硫酸钠、硫酸镁及硫酸钙构成的组中的至少1种,还可以包括选自由硫酸铵、硫酸钠构成的组中的至少1种,也可以是硫酸钠。作为氯化物的具体实施例,例如,可以列举出氯化铵、氯化钾、氯化钠、氯化锂、氯化镁、氯化钙、以及氯化胍等。例如,氯化物可以包括选自由氯化铵、氯化钾、氯化钠、氯化锂、氯化钙、氯化镁及氯化胍构成的组中的至少1种,氯化物也可以包括选自由氯化铵、氯化钾、氯化钠、氯化锂、氯化钙及氯化镁构成的组中的至少1种,氯化物还可以包括选自由氯化钾、氯化钠及氯化钙构成的组中的至少1种,也可以包括选自由氯化钠及氯化钙构成的组中的至少1种,也可以是氯化钠。作为硝酸盐的具体实施例,例如可以列举出硝酸铵、硝酸钾、硝酸钠、硝酸锂、硝酸镁及硝酸钙等。作为碘化物盐的具体实施例,例如可以列举出碘化铵、碘化钾、碘化钠、碘化锂、碘化镁及碘化钙等。作为硫氰酸盐的具体实施例,例如,可以列举出硫氰酸铵、硫氰酸钾、硫氰酸钠、硫氰酸锂、硫氰酸镁、硫氰酸钙、以及硫氰酸胍等。作为碳酸盐的具体实施例,例如可以列举出碳酸铵、碳酸钾、碳酸钠、碳酸锂、碳酸镁及碳酸钙等。作为酸性盐的具体实施例,可以列举出硫酸氢盐、磷酸氢盐及碳酸氢盐等。作为硫酸氢盐的具体实施例,例如可以列举出硫酸氢铵、硫酸氢钾、硫酸氢钠、硫酸氢锂、硫酸氢镁、硫酸氢钙等。作为磷酸氢盐的具体实施例,例如,可以列举出磷酸二氢钠、磷酸氢二钠、磷酸二氢钾、磷酸氢二钾、磷酸二氢铵、磷酸氢二铵、磷酸氢二铵、磷酸二氢镁、磷酸氢二镁、磷酸二氢钙及磷酸氢二钙等。作为碳酸氢盐的具体实施例,例如,可以列举出碳酸氢铵、碳酸氢钾、碳酸氢钠、碳酸氢锂、碳酸氢锂、碳酸氢镁及碳酸氢钙等。作为碱性盐的具体实施例,可以列举出氯化氢氧化钙、氯化氢氧化镁等。上述酸、酸水溶液、盐及盐水溶液可以单独使用1种,也可以混合使用2种以上。作为混合了2种以上的盐或盐水溶液的盐混合水溶液,可以列举出上述有机盐的混合水溶液、上述无机盐的混合水溶液、上述有机盐及无机盐的混合水溶液等,并且从降低制造成本的观点出发,特别优选微咸水及海水。已知微咸水及海水主要包括氯化钾、氯化钠、氯化镁、硫酸镁及硫酸钙。凝固液优选含有盐水溶液,更优选为盐水溶液。通过含有盐,可以进一步提高脱溶剂速度。盐更优选包括由羧酸盐、硫酸盐、氯化物、磷酸氢盐及碳酸氢盐构成的组中的至少1种,进一步优选包括由羧酸盐、硫酸盐及氯化物构成的组中的至少1种,特别优选包括由硫酸盐及氯化物构成的组中的至少1种。通过包括这些盐,可以进一步提高纤维形成能力,并且可以进一步提高所得到的纤维的伸长率。作为羧酸盐,更优选为羧酸钠,作为硫酸盐,更优选为硫酸铵、硫酸钠、硫酸镁及硫酸钙,作为氯化物,更优选氯化钾、氯化钠、氯化镁及氯化钙,作为碳酸氢盐,更优选为碳酸氢钠,作为混合水溶液,特别优选微咸水及海水。通过使用这些盐及混合水溶液,除了具备提高纤维形成能力的效果之外,还可以进一步降低制造成本。相对于凝固液总量,盐含量为0.1质量%以上、0.3质量%以上、0.5质量%以上、0.7质量%以上、1质量%以上、1.3质量%以上、1.5质量%以上、1.7质量%以上、2质量%以上、2.3质量%以上、2.5质量%以上、2.7质量%以上、3质量%以上、4质量%以上、5质量%以上、7质量%以上、10质量%以上、15质量%以上或20质量%以上,作为上限值,可以为30质量%以下、25质量%以下或溶解度以下的含量。例如,相对于凝固液总量,盐含量可以为,0.1质量%以上且30质量%以下、0.3质量%以上且25质量%以下、1质量%以上且25质量%以下、3质量%以上且25质量%以下、5质量%以上且25质量%以下、8质量%以上且25质量%以下、10质量%以上且25质量%以下、1质量%以上且20质量%以下、3质量%以上且20质量%以下、5质量%以上且20质量%以下、8质量%以上且20质量%以下、10质量%以上且20质量%以下、15质量%以上且20质量%以下或16质量%以上且20质量%以下。例如,相对于凝固液总量,盐含量优选为0.05mol/l以上,可以为0.05mol/l以上且5.5mol/l以下,也可以为0.1mol/l以上且5.0mol/l以下,也可以为0.1mol/l以上且4.5mol/l以下,也可以为0.1mol/l以上且4.0mol/l以下。例如,相对于凝固液总量,使用氯化钠时的盐含量可以为0.1mol/l以上且5.0mol/l以下,也可以为0.1mol/l以上且4.5mol/l以下,也可以为0.1mol/l以上且4.0mol/l以下。例如,相对于凝固液总量,使用氯化钾时的盐含量可以为0.1mol/l以上且3.9mol/l以下。例如,相对于凝固液总量,使用氯化钙时的盐含量可以为0.1mol/l以上且14.3mol/l以下,也可以为0.1mol/l以上且13.0mol/l以下,也可以为0.1mol/l以上且12.0mol/l以下,也可以为0.1mol/l以上且11.0mol/l以下,也可以为0.1mol/l以上且10.0mol/l以下,也可以为0.1mol/l以上且9.0mol/l以下,也可以为0.1mol/l以上且8.0mol/l以下,也可以为0.1mol/l以上且7.0mol/l以下,也可以为0.1mol/l以上且6.0mol/l以下,也可以为0.1mol/l以上且5.0mol/l以下,也可以为0.1mol/l以上且4.0mol/l以下,也可以为0.1mol/l以上且3.0mol/l以下,也可以为0.1mol/l以上且2.0mol/l以下。例如,相对于凝固液总量,使用硫酸钠时的盐含量可以为0.1mol/l以上且3.4mol/l以下,也可以为0.1mol/l以上且3.0mol/l以下,也可以为0.1mol/l以上且2.5mol/l以下,也可以为0.1mol/l以上且2.0mol/l以下。此外,例如,相对于凝固液总量,可以为3质量%以上且28质量%以下、3质量%以上且25质量%以下、3质量%以上且20质量%以下、5质量%以上且20质量%以下、8质量%以上且20质量%以下。此外,相对于凝固液总量的硫酸钠的含量优选为10质量%以上且20质量%以下,还优选为11质量%以上且19质量%以下,更优选为11质量%以上且18质量%以下,进一步优选为12质量%以上且18质量%以下,特别优选为12质量%以上且17质量%以下。当硫酸钠相对于凝固液总量的含量为10质量%以上时,可以得到充分的凝固速度,并且可以避免因设备投资引起的费用增加。当硫酸钠相对于凝固液总量的含量为20质量%以下时,可以避免因纺液的急速凝固而引起的在纺液与凝固丝(丝线)之间的界面处发生断丝。此外,从提高溶剂的回收效率的观点出发,在上述情况下,相当于凝固液总量的水含量优选为60质量%以上且80质量%以下,更优选为60质量%以上且70质量%以下。此外,使用硫酸钠时的硫酸钠水溶液的浓度优选为10质量%以上且22质量%以下,还优选为10质量%以上且20质量%以下,更优选为12质量%以上且20质量%以下,进一步优选为14质量%以上且20质量%以下,特别优选为16质量%以上且20质量%以下。当硫酸钠水溶液的浓度为10质量%以上时,可以得到充分的凝固速度,并且可以避免因设备投资引起的费用增加。当硫酸钠水溶液的含量为22质量%以下时,可以避免因纺液的急速凝固而引起的在纺液与凝固丝(丝线)之间的界面处发生断丝。例如,相对于凝固液总量,使用柠檬酸钠时的盐含量可以为0.1mol/l以上且1.6mol/l以下,也可以为0.1mol/l以上且1.3mol/l以下。本实施方式的凝固液中所含的水溶液例如可以选自由羧酸水溶液、碳酸氢盐水溶液、甲酸盐水溶液、乙酸盐水溶液、氯化物水溶液、硫酸盐水溶液、磷酸氢盐水溶液、柠檬酸盐水溶液、微咸水、海水以及它们的混合溶液构成的组。此外,本实施方式的凝固液中所含的水溶液例如可以选自由柠檬酸水溶液、甲酸水溶液、碳酸氢钠水溶液、甲酸钠水溶液、乙酸钠水溶液、氯化钠水溶液、硫酸钠水溶液、硫酸铵水溶液、磷酸氢钾水溶液、氯化钙水溶液、柠檬酸钠水溶液、微咸水、海水以及它们的混合溶液构成的组。与纺丝原液接触前的凝固液中可以含有有机溶剂,也可以不含有机溶剂。此外,即使在与纺丝原液接触前的凝固液中不含有机溶剂的情况下,在使纺丝原液与凝固液接触的过程中,有时会存在有机溶剂从接触的纺丝原液溶解在凝固液中的情形。以凝固液的总质量(当有机溶剂从纺丝原液溶解到凝固液中时,与纺丝原液接触前的凝固液和从纺丝原液溶解到凝固液中的有机溶剂的总含量)为100质量%计,凝固液中所含的有机溶剂(也包括从与凝固液接触的纺丝原液溶解到凝固液中的情况)的含量优选为0质量%以上且40质量%以下、0质量%以上且30质量%以下、5质量%以上且30质量%以下、5质量%以上且25质量%以下、0质量%以上且20质量%以下、5质量%以上且20质量%以下、5质量%以上且15质量%以下、10质量%以上且40质量%以下、15质量%以上且40质量%以下、20质量%以上且40质量%以下、10质量%以上且30质量%以下、10质量%以上且20质量%以下、0质量%以上且10质量%以下、0质量%以上且5质量%以下、0质量%以上且2质量%以下。当有机溶剂的含量在上述范围内时,本申请发明的效果更为显著。以凝固液的总质量为100质量%计,上述凝固液中含有的有机溶剂的含量可以为10质量%以上且40质量%以下,也可以为15质量%以上且40质量%以下,也可以为20质量%以上且40质量%以下。当有机溶剂的含量在上述范围内时,进一步提高了结构蛋白质的纤维形成能力。作为有机溶剂,优选为甲酸、dmso或hfip,更优选为甲酸。凝固液所含的水溶液的ph可以为0.25~10.00,也可以为0.25~9.50。凝固液中的酸水溶液的ph例如可以为0.25~小于7.00,也可以为0.50~小于7.00,也可以为1.00~小于7.00,也可以为1.50~小于7.00,也可以为2.00~小于7.00,还可以为3.00~小于7.00。凝固液中的盐水溶液的ph例如可以是0.50~10.00,也可以是1.00~10.00,也可以是2.00~10.00,也可以是3.00~10.00,也可以是3.50~10.00,也可以是4.00~10.00,也可以是4.50~10.00,也可以是5.00~10.00,也可以是5.50~10.00,也可以是6.00~10.00,也可以是6.50~10.00,还可以是6.50~9.50。相对于凝固液总量,凝固液中的上述水或水溶液的含量优选为60质量%以上,更优选为70质量%以上,更优选为80质量%以上,进一步优选为90质量%以上,特别优选为95质量%以上。当上述水或水溶液的含量在上述范围内时,进一步提高了结构蛋白质的纤维形成能力。相对于凝固液总量,凝固液中的上述水或水溶液的含量例如可以为60质量%以上且100质量%以下,也可以为70质量%以上且100质量%以下,也可以为80质量%以上且100质量%以下,还可以为95质量%以上且100质量%以下。凝固液可以包含甲酸。从提高溶剂回收效率的观点出发,相对于凝固液总量,甲酸的含量优选为15~25质量%,更优选为16~25质量%,进一步优选为16~24质量%,特别优选为18~24质量%。凝固液的温度可以是室温,也可以是0℃~90℃,也可以是0℃~80℃,也可以是5℃~80℃,也可以是10℃~80℃,也可以是15℃~80℃,也可以是20℃~80℃,也可以是25℃~80℃,也可以是30℃~80℃,也可以是40℃~80℃,也可以是50℃~80℃,也可以是60℃~80℃,也可以是70℃~80℃,也可以是20℃~70℃,也可以是30℃~70℃,也可以是40℃~70℃,也可以是50℃~70℃,也可以是20℃~60℃,也可以是30℃~60℃,也可以是40℃~60℃,也可以是50℃~60℃。凝固液的温度的下限值只要在纺丝原液中含有的有机溶剂的熔点以上即可,温度的上限值只要在纺丝原液中含有的有机溶剂的沸点以下即可。通过提高凝固液的温度,可以加快纺丝原液的脱溶剂速度。此外,凝固液的温度优选为55℃~65℃,更优选为45℃~55℃,进一步优选为35℃~45℃。当凝固液的温度为35℃以上时,可以得到适当的脱溶剂速度,并且可以进一步提高生产率。当凝固液的温度为65℃以下,则可以防止因在凝固液中对纺液进行加温而引起的急剧软化。凝固液还可以包含可添加到纺丝原液中的上述溶解促进剂。(纺丝工序)本实施方式所涉及的蛋白质纤维的制备方法可以通过公知的湿式纺丝法及干湿式纺丝法来进行制备。即,在纺丝工序中,使上述纺丝原液与上述凝固液接触,并使蛋白质凝固。包括纺丝工序在内,本实施方式的蛋白质纤维的制备方法例如可以使用图4所示的纺丝装置来实施。图4是示意性地表示用于制备蛋白质纤维的纺丝装置的一例的说明图。图4所示的纺丝装置10是湿式纺丝用的纺丝装置的一例,从上游侧起依次具有挤出装置1、凝固浴槽20、洗涤浴槽(拉伸浴槽)21和干燥装置4。挤出装置1具有储槽7,在此储存有纺丝原液(纺液)6。在凝固浴槽20中储存凝固液11。纺丝原液6通过安装在储槽7的下端部的齿轮泵8,从设置在凝固液11中的喷嘴9挤出。将挤出的纺丝原液6供给(导入)到凝固浴槽20的凝固液11内。在凝固液11内从纺丝原液中除去溶剂,蜘蛛丝蛋白发生凝固。将凝固后的蜘蛛丝蛋白导入至洗涤浴槽21中,通过洗涤浴槽21内的洗涤液12进行洗涤后,由设置在洗涤浴槽21内的第一轧辊13和第二轧辊14将其输送到干燥装置4。此时,例如,如果将第二轧辊14的转速设定地比第一轧辊13的转速快,则可以得到以与转速比相对应的倍率进行拉伸的蛋白质纤维36。在洗涤液12中拉伸后的蛋白质纤维从洗涤浴槽21内脱离后,在通过干燥装置4内时被干燥,然后通过卷线机卷取。如此一来,最终通过纺丝装置10得到蛋白质纤维以作为卷取在卷线机上的卷绕物5。另外,18a~18g是导丝器。凝固液11的温度并没有特别限定,可以为80℃以下、70℃以下、60℃以下、50℃以下、40℃以下、30℃以下、25℃以下、20℃以下、10℃以下或5℃以下。从可操作性、冷却成本等观点出发,优选为0℃以上。另外,凝固液11的温度例如可以通过使用纺丝装置10来进行调整,该纺丝装置具有内部具备热交换器的凝固浴槽20和冷却循环装置。例如,通过使由冷却循环装置冷却到预定温度的介质流过设置在凝固浴槽内的热交换器,能够通过凝固液11和热交换器之间的热交换将温度调整到上述范围内。在这种情况下,通过使作为介质的且用于凝固液11中的溶剂进行循环,可以更有效地进行冷却。储存凝固液的凝固浴槽也可以设置多个。凝固后的人造结构蛋白质可以在脱离凝固浴槽或洗涤浴槽后,直接用卷线机进行卷取,也可以通过干燥装置进行干燥后再用卷线机进行卷取。凝固后的人造结构蛋白质通过凝固液中的距离只要能够高效率地进行脱溶剂即可,其可以根据来自喷嘴的纺丝原液的挤出速度(喷出速度)等来确定。凝固后的人造结构蛋白质(或纺丝原液)在凝固液中的停留时间可以根据凝固后的人造结构蛋白质通过凝固液中的距离、纺丝原液从喷嘴的挤出速度等来确定。(拉伸工序)本实施方式的人造结构蛋白质纤维的制备方法可以进一步包括用于拉伸凝固后的人造结构蛋白质的工序(拉伸工序)。作为拉伸方法,可以列举出湿热拉伸、干热拉伸等。拉伸工序例如可以在凝固浴槽20内实施,也可以在洗涤浴槽21内实施。拉伸工序也可以在空气中实施。在洗涤浴槽21内实施的拉伸也可以是在温水中进行、或在温水中加入有机溶剂等的溶液中等进行的所谓湿热拉伸。湿热拉伸的温度优选为50~90℃。当该温度为50℃以上时,可以稳定地减小丝线的细孔径。此外,当温度为90℃以下时,可以容易地设定温度,并且提高纺丝的稳定性。温度更优选为75~85℃。湿热拉伸可以是在温水中进行、或在温水中加入有机溶剂等的溶液中进行、或在蒸汽加热中进行。作为温度,例如,可以是40~200℃,也可以是50~180℃,也可以是50~150℃,还可以是75~90℃。相对于未拉伸丝(或预拉伸丝),湿热拉伸时的拉伸倍率例如可以为1~30倍,也可以为2~25倍,也可以为2~20倍,也可以为2~15倍,也可以为2~10倍,也可以为2~8倍,也可以为2~6倍,还可以为2~4倍。但是,拉伸倍率只要是在可以得到所希望的纤维的粗细、机械性能等特性的范围内即可,并没有限定。干热拉伸可以通过使用接触式加热板以及非接触式炉子等装置来进行,但是并没有特别限定,只要是能够使纤维升温至预定温度并且以预定的倍率进行拉伸的装置即可。作为温度,例如,可以是100℃~270℃,也可以是140℃~230℃,也可以是140℃~200℃,也可以是160℃~200℃,还可以是160℃~180℃。相对于未拉伸丝(或预拉伸丝),干热拉伸工序中的拉伸倍率例如可以为1~30倍,也可以为2~30倍,也可以为2~20倍,也可以为3~15倍,优选为3~10倍,更优选为3~8倍,进一步优选为4~8倍。但是,拉伸倍率只要是在可以得到所希望的纤维的粗细、机械性能等特性的范围内即可,并没有限定。在拉伸工序中,可以分别单独进行湿热拉伸及干热拉伸,或者也可以将它们分成多个阶段来进行,或者将它们组合进行。即,作为拉伸工序,可以通过湿热拉伸来进行第一阶段拉伸,通过干热拉伸来进行第二阶段拉伸,或者通过湿热拉伸来进行第一阶段拉伸,通过湿热拉伸来进行第二阶段拉伸,进而通过干热拉伸来进行第三阶段拉伸等,可以适当地对湿热拉伸及干热拉伸进行组合。相对于未拉伸丝(或预拉伸丝),经过拉伸工序后的人造结构蛋白质纤维的最终拉伸倍率的下限值优选为1倍、2倍、3倍、4倍、5倍、6倍、7倍、8倍或9倍中的任意一个。经过拉伸工序后的修饰丝心蛋白纤维的最终拉伸倍率的上限值优选为40倍、30倍、20倍、15倍、14倍、13倍、12倍、11倍或10倍中的任意一个。此外,例如,最终拉伸倍率可以为3~40倍,也可以为3~30倍,也可以为5~30倍,也可以为5~20倍,也可以为5~15倍,还可以为5~13倍。但是,拉伸倍率只要是在可以得到所希望的纤维的粗细、机械性能等特性的范围内即可,并没有限定。在纺丝工序中,纺丝喷丝头的喷丝头形状、孔的形状、孔的数量等并没有特别限定,可以根据所希望的纤维直径及单丝根数等来适当地选择。在干燥之前或之后,根据需要,以赋予电荷抑制性能、收敛性能及润滑性等为目的,可以对未拉伸丝(或预拉伸丝)或拉伸丝赋予油剂。所赋予的油剂的种类及赋予的量等并没有特别限定,可以在考虑使用纤维的用途、纤维的可操作性等的基础上进行适当地调整。当纺丝喷丝头的孔形状为圆形时,作为纺丝喷丝头的孔径,可以举例为0.01mm以上且0.6mm以下。当孔径为0.01mm以上时,可以降低压力损失,并且可以抑制设备费用。当孔径为0.6mm以下时,可以降低用于缩小纤维直径的拉伸操作的必要性,并且可以减小在从喷出到卷取之间的过程中发生拉伸断裂的可能性。通过纺丝喷丝头时的纺丝原液的温度及纺丝喷丝头的温度并没有特别限定,可以根据所使用的纺丝原液的浓度及粘度、有机溶剂的种类等进行适当地调整。从防止结构蛋白质发生劣化等的观点出发,该温度优选为30℃~100℃。此外,从降低因溶剂的挥发所引起的压力上升、以及因纺丝原液的凝固所引起的配管内的堵塞的可能性的观点出发,优选地,该温度的上限值小于所使用的溶剂的沸点。由此,提高工序稳定性。本实施方式所涉及的制备方法还可以具备在喷出纺丝原液之前过滤纺丝原液的工序(过滤工序)、及/或在喷出前对纺丝原液进行脱泡的工序(脱泡工序)。(纤维物理性能的评估)可以以如下方式测量和评估人造结构蛋白质纤维的物理性能。在温度为20℃、相对湿度为65%的环境下,使用textechno企业制的单丝强伸测量装置"favimat",测量随机取样的纤维的纤度和强伸度,并计算平均值。测量强伸度的条件优选为:称重传感器容量为210cn,针距长度为20mm,拉伸速度为10mm/min。将断裂时的强度定义为断裂强度[g/d]、将断裂时的伸长率定义为断裂伸长率[%]、将横轴设为应变[%]、将纵轴设为应力[g/d]时的由应力-应变曲线和横轴所包围的面积的数值乘以密度[kg/m3]而得到的值定义为韧性[mj/m3]。优选地,将测量值作为例如采样数n=10的平均值进行计算。(纤维收缩性的评估)人造结构蛋白质纤维具有通过与低于沸点的水接触(湿润)而收缩的特性。在人造结构蛋白质纤维中,这样的收缩越少优选度越高。收缩性例如可以将通过以下方法求出的收缩率作为指标来评估。将长度约30cm的多根人造结构蛋白质纤维集束在一起,制成纤度为150旦的纤维束。在此纤维束上安装重量为0.8g的铅锤,在此状态下将纤维束浸渍在40℃的水中90秒以使其收缩。然后,从水中取出各个纤维束,在安装重量为0.8g的铅锤的状态下使其干燥,并且测量干燥后的各个纤维束的长度。收缩率根据下式进行计算。另外,l0表示与水接触前(纺丝后)的纤维长度(在这种情况为30cm),ld表示收缩后(在水中进行浸渍处理后的干燥纤维)的纤维的长度。式:收缩率[%]={1-(ld/l0)}×100(产品)本实施方式所涉及的蛋白质纤维作为纤维(长纤维、短纤维、单丝或复丝等)或丝线(纺织丝、捻丝、假捻丝、加工丝、混纤丝或混纺丝等),其可以应用于织物、针织物、编织物或无纺布等布帛、纸及棉等中。此外,还可以应用于绳索、手术用缝合线、止血剂、电气部件用的可挠性紧固件、以及移植用生理活性材料(例如,人造韧带及主动脉带)等高强度用途中。这些可以通过公知的方法来制备。实施例下面,将基于实施例更具体地说明本发明。但是,本发明并不限于以下实施例。(人造结构蛋白质的制备)(1)表达载体的制备根据来自于金纺蜘蛛(nephilaclavipes)的丝心蛋白(genbank登录号:p46804.1、gi:1174415)的碱基序列及氨基酸序列,对具有序列号44的人造结构蛋白质(修饰丝心蛋白)(以下也称为“prt966”。)、具有序列号15的修饰丝心蛋白(以下也称为“prt799”。)、具有序列号37的修饰丝心蛋白(以下也称为“prt918”。)、具有序列号50的修饰丝心蛋白(以下也称为“prt705”。)、具有序列号51的修饰丝心蛋白(以下也称为“prt826”。)、具有序列号52的修饰丝心蛋白(以下也称为“prt853”。)、具有序列号53的修饰丝心蛋白(以下也称为“prt1103”。)、具有序列号54的修饰丝心蛋白(以下也称为“prt1104”。)、具有序列号55的修饰丝心蛋白(以下也称为“prt1107”。)、具有序列号56的修饰丝心蛋白(以下也称为“prt1083”)及具有序列号57的修饰丝心蛋白(以下也称为“prt1125”。)进行设计。此外,作为人造结构蛋白质,包括具有序列号58的角蛋白(以下也称为"prt855"。)、具有序列号59的胶原蛋白(以下也称为"prt537"。)、具有序列号60的节肢弹性蛋白质(以下也称为"prt366"。)及具有排序列号61的干扰素γ(以下也称为"prt662"。)。另外,序列号44所示的氨基酸序列以提高疏水性为目的,具有将序列号9所示的氨基酸序列(在c末端附加序列号42所示的氨基酸序列之前的氨基酸序列)中的qq全部置换为vf、并且将其余的q置换为i的氨基酸序列,进而在n末端添加序列号12所示的氨基酸序列。此外,序列号15所示的氨基酸序列具有为了提高生产率而对来自于金纺蜘蛛的丝心蛋白的氨基酸序列进行氨基酸残基的置换、插入及缺失的氨基酸序列,进而在n末端添加序列号12所示的氨基酸序列(标签序列及铰链序列)。序列号53所示的氨基酸序列(prt1103)是在将序列号7(met-prt410)所示的氨基酸序列的酪氨酸残基(y)置换为苯丙氨酸残基(f)、并且将丝氨酸残基(s)中的大部分置换为丙氨酸残基(a)或甘氨酸残基(g)的序列中,进一步在n末端添加标签序列的序列。在序列号54所示的氨基酸序列(prt1104)中,将序列号7所示的氨基酸序列的丝氨酸残基(s)的大部分置换为丙氨酸残基(a)或甘氨酸残基(g),并进一步在n末端添加标签序列。在序列号55所示的氨基酸序列(prt1107)中,将序列号31所示的氨基酸序列(met-prt918)的丝氨酸残基(s)置换为丙氨酸残基(a)、缬氨酸残基(v)、亮氨酸残基(l)或异亮氨酸残基(i),并进一步在n末端添加标签序列。在序列号56所示的氨基酸序列(prt1083)中,将序列号31所示的氨基酸序列(met-prt918)的脯氨酸残基(p)置换为苏氨酸残基(t)或亮氨酸残基(l),并进一步在n末端添加标签序列。序列号58所示的氨基酸序列(prt855)相对于prt798(序列号49)的从n末端起的第1~292个氨基酸残基组成的氨基酸序列、以及将亮氨酸或缬氨酸置换成丙氨酸或甘氨酸的氨基酸序列,具有对从n末端起的第1~246个氨基酸残基中的3个氨基酸残基进行置换、以及对插入由gaaaaag(序列号62)构成的氨基酸序列后得到的氨基酸序列进行重复的氨基酸序列。接下来,对编码所设计的人造结构蛋白质prt966、prt799、prt918、prt826、prt853、prt1104、prt705、prt1125、prt1103、prt1107及prt1083(修饰丝心蛋白)、prt855(角蛋白)、prt537(胶原蛋白)、prt366(节肢弹性蛋白质)以及干扰素γ(prt662)的核酸进行合成。在该核酸中,在5末端添加ndei位点,并在终止密码子的下游添加ecori位点。将该核酸克隆到克隆载体(puc118)上。然后,通过用ndei及ecori对该核酸进行限制酶处理并进行切出后,分别重组为蛋白质表达载体pet-22b(+),以得到表达载体。(2)人造结构蛋白质的表达用(1)中所得到的表达载体转化大肠杆菌blr(de3)。将该转化的大肠杆菌在含有氨苄青霉素的2mllb培养基中培养15小时。将该培养液以od600为0.005的方式添加到含有氨苄青霉素的100ml种子培养用培养基(表5)中。将培养液温度保持在30℃,进行烧瓶培养直到od600变为5(约15小时),以得到种子培养液。[表5]将该种子培养液以od600为0.05的方式添加到添加了500ml的生产培养基(表6)的小型发酵罐。将培养液温度保持在37℃,将ph恒定控制在6.9下进行培养。此外,将培养液中的溶解氧浓度维持在溶解氧饱和浓度的20%。[表6]在生产培养基中的葡萄糖完全消耗后,马上以1ml/分钟的速度添加进料液(葡萄糖455g/1l、yeatextract120g/1l)。将培养液温度保持在37℃,将ph恒定控制在6.9下进行培养。此外,将培养液中的溶解氧浓度维持在溶解氧饱和浓度的20%,培养20小时。然后,向培养液中添加1m的异丙基-β-硫代半乳糖吡喃糖苷(iptg)以使其最终浓度为1mm,并表达诱导修饰丝心蛋白。在添加iptg后经过20个小时,离心分离培养液,并且回收菌体。使用由iptg添加前和iptg添加后的培养液制备的菌体进行sds-page,通过取决于iptg添加的目标修饰丝心蛋白大小的条带的出现,确认目标人造结构蛋白质的表达。(3)人造结构蛋白质的纯化将自添加iptg起2小时后回收的菌体用20mmtris-hclbuffer(ph7.4)洗涤。将洗涤后的菌体悬浮在含有约1mm的pmsf的20mmtris-hcl缓冲液(ph7.4)中,用高压均质器(geanirosoavi企业制)来破碎细胞。对破碎后的细胞进行离心分离,得到沉淀物。将得到的沉淀物用20mmtris-hcl缓冲液(ph7.4)洗涤,直至达到高纯度为止。将洗涤后的沉淀物以达到100mg/ml的浓度的方式在8m胍缓冲液(8m盐酸胍、10mm磷酸二氢钠、20mmnacl、1mmtris-hcl、ph7.0)中悬浮,并在60℃下用搅拌器搅拌30分钟,以使其溶解。溶解后,使用透析管(三光纯药株式会社制的纤维素管36/32)用水进行透析。通过离心分离来回收透析后得到的白色聚集蛋白质,用冷冻干燥机除去水分,回收冷冻干燥粉末,由此得到修饰丝心蛋白(prt966、prt799、prt918prt826、prt853、prt1104、prt705、,prt1125、prt1103、prt1107及prt1083)、prt855(角蛋白)、prt537(胶原蛋白)、prt366(节肢弹性蛋白)以及prt662(干扰素γ)。(纤维形成能力的评估(凝固液))(1-1)纺液的制备将在上述人造结构蛋白质的制备工序中得到的修饰丝心蛋白(prt966)26质量%、和作为溶解用溶剂的甲酸(株式会社朝日化学企业制,纯度98%)74质量%进行混合,边搅拌边用70℃的铝块加热器加热1小时,以使其溶解。用网孔为1μm的金属过滤器过滤、脱泡,以得到纺液。(1-2)纺液的喷出试验将(1-1)中得到的纺液填充到10ml的注射器中,并从喷嘴直径为0.2μm的喷嘴喷出至凝固液中,以在室温下凝固修饰丝心蛋白。凝固的原纤维以2.39m/min的线速度进行卷取。观察所得到的原纤维,并且目视判断纤维形成能力。纺液的挤出速度为0.075ml/分钟。所使用的凝固液的种类如表7所示。另外,微咸水是在山形县酒田市的河口部采集的微咸水,海水是从山形县加茂市的海洋采集的海水。微咸水及海水的浓度[wt%]表示所有溶质浓度的近似值。试验例26~28的混合溶液是假设将所接触的纺丝原液中的甲酸溶解于氯化钠水溶液中,并将凝固液的总质量(混合溶液)的比例设为氯化钠水溶液60质量%~80质量%及甲酸20质量%~40质量%的溶液。试验例29的甲酸水溶液是假设将所接触的纺丝原液中的甲酸溶解于水中,并将凝固液的总质量(混合溶液)的比例设为水80质量%及甲酸20质量%的溶液。纤维形成能力的评估结果如表7所示。纤维形成能力的评估标准如下所示。⊙:形成纤维。所得纤维具有可挠性,并且是均质的。○:形成纤维。所得纤维具有可挠性。△:形成纤维。×:没有形成纤维。[表7]如表7所示,当使用水、酸水溶液、盐水溶液及混合溶液中的任意1种时,都可以形成具有可挠性的纤维(试验例1~试验例26)。当凝固液为盐水溶液时,可以形成具有可挠性且均质的纤维,并且显示出极其良好的纤维形成能力(试验例4~试验例26)。特别是,通过在凝固液中使用资源丰富且低价的水、氯化钠水溶液、微咸水以及海水,可以大幅度地降低制造成本。此外,显示出即使当所接触的纺丝原液中的有机溶剂溶解在凝固液中时,也可以形成具有可挠性的纤维(试验例27~试验例30)。特别是当溶解有甲酸的凝固液为氯化钠水溶液时,可以形成具有可挠性且均质的纤维(试验例28~试验例30)。(纤维形成能力的评估(蛋白质))(2-1)纺液的制备对在上述人造结构蛋白质的制备工序中得到的修饰丝心蛋白(prt966、prt826、prt853、prt1104、prt705、prt1125、prt1103、prt1107及prt1083)、角蛋白(prt855)、胶原蛋白(prt537)和节肢弹性蛋白(prt366)或干扰素γ(prt662)26质量%或作为市售的结构蛋白质的medigelatin(株式会社nippi制)、蛋清白蛋白或酪蛋白26质量%,和含有作为溶解用溶剂的甲酸74质量%或氯化锂的二甲基亚砜溶液(氯化锂浓度:4.0质量%)74质量%进行混合,边搅拌边用70℃的铝块加热器加温1小时,以使其溶解。用网孔为1μm的金属过滤器过滤、脱泡,以得到纺液。表8示出了所制备的纺液。(2-2)纺液的喷出试验将(2-1)中得到的纺液填充到10ml的注射器中,并从喷嘴直径为0.2μm的喷嘴喷出至凝固液(浓度30%的硫酸钠水溶液或水)中,以在室温下凝固修饰丝心蛋白。观察所得到的原纤维,并且目视判断纤维形成能力。纺液的挤出速度为0.075ml/分钟。纤维形成能力的评估标准如下所示。纤维形成能力的评估结果如表8所示。另外,表8中的平均hi是求出构成结构蛋白质的所有氨基酸残基的疏水性指标(hi)的总和,然后将此总和除以氨基酸残基总数而计算出的值。其是通过计算序列表中所记载的氨基酸序列(包含标签序列或铰链序列的序列)的疏水性指标而计算出的值。○:形成纤维,凝固性良好。△:形成纤维,但是凝固性低。×:纺液凝胶化或溶质不可溶解[表8]如表8所示,当凝固液为硫酸钠水溶液的情况下,确认了在平均hi值为-1.229~0.95的所有结构蛋白质中形成纤维,并且具有纤维形成能力(试验例83~109)。更进一步地,当凝固液为水的情况下,确认了在平均hi值为0.466~0.95的修饰丝心蛋白中形成纤维,并且具有纤维形成能力(试验例107~109)。当凝固液中使用硫酸钠水溶液的情况下,显示出无论结构蛋白质的种类如何,都可以形成纤维,并且具有优异的纤维形成能力。(人造结构蛋白质纤维的制备及评估)(1)纺液的制备除了将修饰丝心蛋白(prt966)的浓度设为26质量%、并且将甲酸的浓度设为74质量%以外,按照与在上述纤维形成能力的评估中所制备的纺液相同的步骤来制备纺液。(2)湿式纺丝将制备的纺液填充到储藏罐中,使用台式纺丝装置从直径为0.2mm的单孔喷嘴中使用齿轮泵在凝固浴槽中喷出,并形成原丝。接下来,将凝固的原丝在水浴中拉伸。在水浴中进行洗涤及拉伸后,使用干燥板进行干燥,并且使用台式纺丝装置卷曲所得到的修饰丝心蛋白纤维(人造蛋白质纤维)。湿式纺丝的条件如下,所使用的凝固液如表9所示。挤出喷嘴直径:0.2mm凝固液的温度:室温水浴中的拉伸倍率:3.5~5.5倍水浴的温度:40℃干燥温度:60℃(3)人造结构蛋白质纤维的物理性能评估通过以下方法来测量在上述(2)中所得到的纤维的物理性能。在温度为20℃、相对湿度为65%的环境下,使用textechno企业制的单丝强伸测量装置"favimat",测量随机取样的10根纤维的纤度和强伸度(采样数=10),并计算出平均值。测量强伸度的条件为:称重传感器容量为210cn,针距长度为20mm,拉伸速度为10mm/min。将断裂时的强度定义为断裂强度[g/d],并且将断裂时的伸长率定义为断裂伸长率[%]。此外,将横轴设为应变[%]、将纵轴设为应力[g/d]时的由应力-应变曲线和横轴所包围的面积的数值乘以密度[kg/m3]而得到的值定义为韧性[mj/m3]。修饰丝心蛋白(prt966)的密度为1.34[g/cm3]。各修饰丝心蛋白纤维的机械物理性能评估结果如表9、表10、表11及表12所示。表9及表10中的伸长率的值是将比较例2(在凝固浴中使用甲醇100%来制备的纤维)中的修饰丝心蛋白纤维的断裂伸长率的值设为100时的相对值。另外,关于表9的试验例33(氯化钾水溶液)及试验例36(硫酸钠水溶液)、以及表10的断裂伸长率,示出了将凝固浴温度设为60℃时的值。表11及表12中的韧性值是将比较例3(在凝固浴中使用甲醇100%来制备的纤维)中的修饰丝心蛋白纤维的韧性设为100时的相对值。另外,关于表11的试验例44(氯化钾水溶液)及试验例47(硫酸钠水溶液)、以及表12的韧性的相对值,示出了将凝固浴温度设为60℃时的值。[表9]如表9所示,在凝固液中使用羧酸盐水溶液(柠檬酸钠及甲酸钠水溶液)、氯化物水溶液(氯化钾、氯化钠及氯化钙水溶液)、硫酸盐水溶液(硫酸钠及硫酸铵水溶液)、磷酸氢盐水溶液(缓冲液)、以及混合溶液(微咸水及海水)制备而成的修饰丝心蛋白纤维(试验例31~试验例40)及在凝固液中使用水制备而成的修饰丝心蛋白纤维(试验例41),与在凝固液中使用甲醇制备而成的修饰丝心蛋白纤维(比较例2)进行比较,均具有进一步提高伸长率的效果,并且可以得到预想不到的优异结果。[表10]如表10所示,在凝固液中使用氯化钠水溶液和甲酸的混合水溶液制备而成的修饰丝心蛋白纤维(试验例43~44)及在凝固液中使用水和甲酸的混合水溶液制备而成的修饰丝心蛋白纤维(试验例45~46),与在凝固液中使用甲醇制备而成的修饰丝心蛋白纤维(比较例2)进行比较,在任何一种混合比例下,均具有进一步提高伸长率的效果,并且可以得到预想不到的优异结果。由此可知,即使将纺丝原液的甲酸溶解于水(试验例41)及氯化钠水溶液的凝固液(试验例42)的情况下,也可以确认到优异的伸长率改善效果。[表11]如表11所示,在凝固液中使用羧酸盐水溶液(柠檬酸钠水溶液及甲酸钠水溶液)、氯化物水溶液(氯化钾水溶液及氯化钠水溶液)、硫酸盐水溶液(硫酸钠水溶液及硫酸铵水溶液)、磷酸水盐的缓冲液、以及混合溶液(微咸水及海水)制备而成的修饰丝心蛋白纤维(试验例47~试验例56)及在凝固液中使用水制备而成的修饰丝心蛋白纤维(试验例56),与在凝固液中使用甲醇制备而成的修饰丝心蛋白纤维(比较例3)进行比较,均具有进一步提高韧性值的效果,并且可以得到预想不到的优异结果。[表12]如表12所示,在凝固液中使用氯化钠水溶液及甲酸的混合水溶液制备而成的修饰丝心蛋白纤维(试验例58~59)及在凝固液中使用水和甲酸的混合水溶液制备而成的修饰丝心蛋白纤维(试验例60~61),与在凝固液中使用甲醇制备而成的修饰丝心蛋白纤维(比较例3)进行比较,在任何一种混合比例下,均具有进一步提高韧性值的效果,并且可以得到预想不到的优异结果。由此可知,即使将纺丝原液的甲酸溶解于水(试验例41)及氯化钠水溶液的凝固液(试验例34)的情况下,也可以确认到优异的韧性值改善效果。(4)人造结构蛋白质纤维的收缩性评估将上述(2)中得到的修饰丝心蛋白纤维聚拢成长度约30cm并进行捆束,以得到纤度为150d的丝心蛋白纤维束。在各丝心蛋白纤维束上安装重量为0.8g的铅锤,并且在此状态下将纤维束浸渍在40℃的水中90秒以使其收缩。然后,从水中取出各个纤维束,在安装重量为0.8g的铅锤的状态下使其干燥,并且测出干燥后的各个纤维束的长度。根据下式计算出收缩率。另外,l0表示与水接触前(纺丝后)的修饰丝心蛋白纤维的长度(在这种情况为30cm),ld表示收缩后(在水中进行浸渍处理后的干燥纤维)的纤维的长度。式:收缩率[%]={1-(ld/l0)}×100各修饰丝心蛋白纤维的收缩率如表11及表12所示。将比较例4(在凝固浴中使用甲醇来制备的纤维)中的修饰丝心蛋白纤维的收缩率的值(17.0%)设为100时的相对值以示出表13及表14中的收缩率的值。另外,关于表13的试验例64(氯化钾水溶液)及试验例73(硫酸钠水溶液)、以及表14的收缩率,示出了将凝固浴温度设为60℃时的值。[表13]如表13所示,在凝固液中使用羧酸盐水溶液(柠檬酸钠水溶液及甲酸钠水溶液)、氯化物水溶液(氯化钾水溶液及氯化钠水溶液)、硫酸盐水溶液(硫酸钠水溶液及硫酸铵水溶液)、磷酸水盐水溶液、以及混合溶液(微咸水及海水)制备而成的修饰丝心蛋白纤维(试验例62~76)以及在凝固液中使用水制备而成的修饰丝心蛋白纤维(试验例77),与在凝固液中使用甲醇制备而成的修饰丝心蛋白纤维(比较例4)进行比较,具有降低对水的收缩率的优异效果,可以得到预想不到的优异结果。特别是,通过在凝固液中使用资源丰富且低价的水、氯化钠水溶液、硫酸钠水溶液,微咸水以及海水,除了可以大幅度地降低制造成本之外,还可以获得提高伸长率的效果(参照表9)、改善韧性的效果(参照表11)、以及降低对水分的收缩性的效果(参照表13)。[表14]如表14所示,在凝固液中使用氯化钠水溶液及甲酸的混合水溶液制备而成的修饰丝心蛋白纤维(试验例78~80)及在凝固液中使用水和甲酸的混合水溶液制备而成的修饰丝心蛋白纤维(试验例81~82),与在凝固液中使用甲醇制备而成的修饰丝心蛋白纤维(比较例4)进行比较,在任何一种混合比例下,均具有降低对水的收缩率的优异效果,可以得到预想不到的优异结果。由此可知,即使将纺丝原液的甲酸溶解于水(试验例77)及氯化钠水溶液的凝固液(试验例65)的情况下,也可以确认具有降低对水的收缩率的优异效果。参考例1:修饰丝心蛋白的燃烧性试验将修饰丝心蛋白(prt799)的冷冻干燥粉末添加至氯化锂的二甲基亚砜溶液(浓度:4.0质量%)中以使其浓度为24质量%,并使用振荡器混合3小时,以使其溶解。然后,除去不溶物和气泡,得到修饰丝心蛋白溶液(纺丝原液)。将得到的纺丝原液加热至90℃,用网孔为5μm的金属过滤器过滤,然后将其放入30ml的不锈钢注射器内静置并使其脱泡后,从针头直径为0.2mm的实心喷嘴喷出至100质量%的甲醇凝固浴槽中。喷出温度为90℃。凝固后,卷取所得到的原丝并使其自然干燥,以得到修饰丝心蛋白纤维(原料纤维)。使用将原料纤维捻合在一起的捻丝,通过使用圆形针织机进行圆形编织来制造针织物(粗细:180旦,针距:18)。将得到的针织物切出20g,以作为试验片使用。燃烧性试验依据"消防厅危险物规制第50号(1995年5月31日)"中记载的"粉粒状或低熔点的合成树脂的试验方法"。试验在温度为22℃、相对湿度为45%、气压为1021hpa的条件下实施。测量结果(氧气浓度(%)、燃烧率(%)、燃烧转化率(%))如表15所示。[表15]氧气浓度(%)燃烧率(%)燃烧转化率(%)20.039.140.127.048.149.327.051.953.230.053.654.950.061.262.770.091.193.3100.097.6100.0作为燃烧性试验的结果,用修饰丝心蛋白(prt799)纤维编织的针织物的临界氧指数(loi)值为27.2。通常,已知loi值为26以上时,其具有阻燃性。由此可知修饰丝心蛋白的阻燃性优异。参考例2:修饰丝心蛋白的吸湿发热性能评估将修饰丝心蛋白的冷冻干燥粉末添加至氯化锂的二甲基亚砜溶液(浓度:4.0质量%)中以使其浓度为24质量%,并使用振荡器混合3小时,以使其溶解。然后,除去不溶物和气泡,得到修饰丝心蛋白溶液(纺丝原液)。将得到的纺丝原液加热至60℃,用网孔为5μm的金属过滤器过滤,然后将其放入30ml的不锈钢注射器内静置并使其脱泡后,从针头直径为0.2mm的实心喷嘴喷出至100质量%的甲醇凝固浴槽中。喷出温度为60℃。凝固后,卷取所得到的原丝并使其自然干燥,以得到修饰丝心蛋白纤维(原料纤维)。为了比较,准备市售的羊毛纤维、棉纤维、天丝纤维、人造纤维及涤纶纤维以作为原料纤维。使用各种原料纤维,通过使用横编织机进行横编织来分别制造针织物。使用prt918纤维或prt799纤维的针织物的粗细及针距如表16所示。调整使用了其他原料纤维的针织物的粗细及针距,以使其具有与修饰丝心蛋白纤维的针织物大致相同的覆盖因子。具体而言,如下所述。[表16]原料纤维粗细[n]针距[gg]prt9181/30(毛纱支数单丝)18prt7991/30(毛纱支数单丝)16羊毛2/30(双丝)14棉布2/34(双丝)14天丝2/30(双丝)15人造纤维1/38(单丝)14涤纶1/60(单丝)14将2块裁剪为10cm×10cm的针织物贴合在一起,将四边缝合,以制成试验片(试样)。将试验片在低湿环境(温度20±2℃,相对湿度40±5%)下放置4小时以上后,移至高湿度环境(温度20±2℃,相对湿度90±5%),利用安装于试验片内部中央的温度传感器以1分钟间隔进行30分钟的温度测量。根据测量结果,按照下述式a来求出最大吸湿发热度。式a:最高吸湿发热度={(将试样置于低湿度环境下直至试样温度达到平衡后,将其移至高湿度环境下时的试样温度的最高值)-(将试样置于低湿度环境下直至试样温度达到平衡后,将其移至高湿度环境下时的试样温度)}(℃)/试样重量(g)图5是表示吸湿发热性能试验的结果的一例的图表。图表的横轴表示在高湿度环境下的放置时间(分钟),其中0为试样从低湿环境转移到高湿度环境的时间。图表的纵轴表示由温度传感器测量的温度(试样温度)。在图5所示的图表中,由m表示的点对应于试样温度的最高值。各针织物的最大吸湿发热度的计算结果如表16所示。[表17]如表17所示,可知修饰丝心蛋白(prt918及prt799)与现有的材料相比,最大吸湿发热度高,并且吸湿发热性能优异。参考例3:修饰丝心蛋白的保温性能评估将修饰丝心蛋白的冷冻干燥粉末添加至氯化锂的二甲基亚砜溶液(浓度:4.0质量%)中以使其浓度为24质量%,并使用振荡器混合3小时,以使其溶解。然后,除去不溶物和气泡,得到修饰丝心蛋白溶液(纺丝原液)。将得到的纺丝原液加热至60℃,用网孔为5μm的金属过滤器过滤,然后将其放入30ml的不锈钢注射器内静置并使其脱泡后,从针头直径为0.2mm的实心喷嘴喷出至100质量%的甲醇凝固浴槽中。喷出温度为60℃。凝固后,卷取所得到的原丝并使其自然干燥,以得到修饰丝心蛋白纤维(原料纤维)。为了比较,准备市售的羊毛纤维、丝绸纤维、棉纤维、人造纤维及涤纶纤维以作为原料纤维。使用各种原料纤维,通过使用横编织机进行横编织来分别制造针织物。使用prt966纤维或prt799纤维的针织物的支数、捻根数、针距及单位面积重量如表18所示。调整使用了其他原料纤维的针织物,以使其具有与修饰丝心蛋白纤维的针织物大致相同的覆盖因子。具体而言,如下所述。[表18]原料纤维支数[nm]捻根数针距[gg]单位面积重量[g/m2]prt9663011890.1prt79930116111.0羊毛30214242.6丝绸60214225.2棉布34214194.1人造纤维38114181.8涤纶60114184.7保温性能使用加多技术有限企业制的kes-f7thermolabii试验机,并使用干式接触法(假设皮肤和衣服以干燥状态直接接触时的方法)进行评估。将一块裁剪为20cm×20cm的矩形的针织物作为试验片(试样)使用。将试验片设置在设定为恒温(30℃)的热板上,在风洞内风速为30cm/秒的条件下,求出通过试验片散发的热量(a)。在不设置试验片的状态下,求出在与上述条件相同的条件下所散发的热量(b),并且根据下述式b计算出保温率(%)。式b:保温率(%)=(1-a/b)×100根据测量结果,按照下述式c,求出保温性能指数。式c:保温性能指数=保温率(%)/试样的单位面积重量(g/m2)保温性能指数的计算结果如表18所示。可以评估出材料的保温性能指数越高,保温性能就越优异。[表19]原料纤维保温性能指数prt9660.33prt7990.22羊毛0.16丝绸0.11棉布0.13人造纤维0.02涤纶0.18如表19所示,可知修饰丝心蛋白(prt966及prt799)与现有的材料相比,保温性能指数高,并且保温性能优异。如参考例1~3所示,当修饰丝心蛋白为修饰蛛丝类丝心蛋白时,可以使保温性能、吸湿发热性能及/或阻燃性更优异。当使用修饰蛛丝类丝心蛋白作为蛋白质,并在凝固液中使用水或ph为0.25以上且ph为10.00以下的水溶液(特别是氯化钠水溶液、硫酸钠水溶液、硫酸铵水溶液、氯化钾水溶液、氯化钙水溶液、甲酸钠水溶液、柠檬酸钠水溶液、甲酸水溶液、甲酸的混合水溶液、微咸水及海水)制成纤维时,可以得到保温性能、吸湿发热性能及/或阻燃性、韧性以及伸长率更为优异、并且可以进一步降低对水分的收缩率的纤维。符号说明1挤出装置2未拉伸丝制造装置3湿热拉伸装置4干燥装置6纺丝原液10纺丝装置20凝固浴槽21洗涤浴槽36蛋白质纤维序列表<110>丝芭博株式会社<120>蛋白质纤维的制备方法<130>fp19-0989-00<150>jp2018-185598<151>2018-09-28<160>62<170>patentinversion3.5<210>1<211>50<212>prt<213>十字园蛛<400>1serglycysaspvalleuvalglnalaleuleugluvalvalserala151015leuvalserileleuglyserserserileglyglnileasntyrgly202530alaseralaglntyrthrglnmetvalglyglnservalalaglnala354045leuala50<210>2<211>30<212>prt<213>十字园蛛<400>2serglycysaspvalleuvalglnalaleuleugluvalvalserala151015leuvalserileleuglyserserserileglyglnileasn202530<210>3<211>21<212>prt<213>十字园蛛<400>3serglycysaspvalleuvalglnalaleuleugluvalvalserala151015leuvalserileleu20<210>4<211>1154<212>prt<213>人工序列<220><223>重组蛛丝蛋白adf3kailargenrsh1<400>4methishishishishishishishishishisserserglyserser151015leugluvalleupheglnglyproalaargalaglyserglyglngln202530glyproglyglnglnglyproglyglnglnglyproglyglnglngly354045protyrglyproglyalaseralaalaalaalaalaalaglyglytyr505560glyproglyserglyglnglnglyproserglnglnglyproglygln65707580glnglyproglyglyglnglyprotyrglyproglyalaseralaala859095alaalaalaalaglyglytyrglyproglyserglyglnglnglypro100105110glyglyglnglyprotyrglyproglyserseralaalaalaalaala115120125alaglyglyasnglyproglyserglyglnglnglyalaglyglngln130135140glyproglyglnglnglyproglyalaseralaalaalaalaalaala145150155160glyglytyrglyproglyserglyglnglnglyproglyglnglngly165170175proglyglyglnglyprotyrglyproglyalaseralaalaalaala180185190alaalaglyglytyrglyproglyserglyglnglyproglyglngln195200205glyproglyglyglnglyprotyrglyproglyalaseralaalaala210215220alaalaalaglyglytyrglyproglyserglyglnglnglyprogly225230235240glnglnglyproglyglnglnglyproglyglyglnglyprotyrgly245250255proglyalaseralaalaalaalaalaalaglyglytyrglyprogly260265270tyrglyglnglnglyproglyglnglnglyproglyglyglnglypro275280285tyrglyproglyalaseralaalaseralaalaserglyglytyrgly290295300proglyserglyglnglnglyproglyglnglnglyproglyglygln305310315320glyprotyrglyproglyalaseralaalaalaalaalaalaglygly325330335tyrglyproglyserglyglnglnglyproglyglnglnglyprogly340345350glnglnglyproglyglnglnglyproglyglyglnglyprotyrgly355360365proglyalaseralaalaalaalaalaalaglyglytyrglyprogly370375380serglyglnglnglyproglyglnglnglyproglyglnglnglypro385390395400glyglnglnglyproglyglnglnglyproglyglnglnglyprogly405410415glnglnglyproglyglnglnglyproglyglnglnglyproglygly420425430glnglyalatyrglyproglyalaseralaalaalaglyalaalagly435440445glytyrglyproglyserglyglnglnglyproglyglnglnglypro450455460glyglnglnglyproglyglnglnglyproglyglnglnglyprogly465470475480glnglnglyproglyglnglnglyproglyglnglnglyprotyrgly485490495proglyalaseralaalaalaalaalaalaglyglytyrglyprogly500505510serglyglnglnglyproglyglnglnglyproglyglnglnglypro515520525glyglyglnglyprotyrglyproglyalaalaseralaalavalser530535540valserargalaargalaglyserglyglnglnglyproglyglngln545550555560glyproglyglnglnglyproglyglnglnglyprotyrglyprogly565570575alaseralaalaalaalaalaalaglyglytyrglyproglysergly580585590glnglnglyproserglnglnglyproglyglnglnglyproglygly595600605glnglyprotyrglyproglyalaseralaalaalaalaalaalagly610615620glytyrglyproglyserglyglnglnglyproglyglyglnglypro625630635640tyrglyproglyserseralaalaalaalaalaalaglyglyasngly645650655proglyserglyglnglnglyalaglyglnglnglyproglyglngln660665670glyproglyalaseralaalaalaalaalaalaglyglytyrglypro675680685glyserglyglnglnglyproglyglnglnglyproglyglyglngly690695700protyrglyproglyalaseralaalaalaalaalaalaglyglytyr705710715720glyproglyserglyglnglyproglyglnglnglyproglyglygln725730735glyprotyrglyproglyalaseralaalaalaalaalaalaglygly740745750tyrglyproglyserglyglnglnglyproglyglnglnglyprogly755760765glnglnglyproglyglyglnglyprotyrglyproglyalaserala770775780alaalaalaalaalaglyglytyrglyproglytyrglyglnglngly785790795800prog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