CAJ | 학술논문

利用傅里叶变换拉曼光谱技术对不同吐丝环境下获得的棒络新妇蜘蛛牵引丝(自由爬行分泌的牵引丝,垂直下落时分泌的牵引丝,在20 mm·s-1的速度下人工强制抽取的牵引丝)纤维大分子结构进行了分析,对特征谱带的分析结果表明,蜘蛛牵引丝蛋白中包含了β-折叠,β-转角,α-螺旋以及无规卷曲结构;酰胺I带中,不同的方式获得的牵引丝中所含的4种二级结构的比例不同.其中人工强制抽取获得的牵引丝中包含较多的β-折叠结构,α-螺旋含量最少,说明在不同环境条件下,蜘蛛分泌牵引丝的结构会发生变化,这一改变可能会导致丝纤维的力学特性的改变.
이용부리협변환랍만광보기술대불동토사배경하획득적봉락신부지주견인사(자유파행분비적견인사,수직하락시분비적견인사,재20 mm·s-1적속도하인공강제추취적견인사)섬유대분자결구진행료분석,대특정보대적분석결과표명,지주견인사단백중포함료β-절첩,β-전각,α-라선이급무규권곡결구;선알I대중,불동적방식획득적견인사중소함적4충이급결구적비례불동.기중인공강제추취획득적견인사중포함교다적β-절첩결구,α-라선함량최소,설명재불동배경조건하,지주분비견인사적결구회발생변화,저일개변가능회도치사섬유적역학특성적개변.
Raman spectra of Nephia clavata spider dragline silk fibers were obtained by three different spin-ning methods:crawl spinning, drop spinning and artificial reeling at 20 mm/s. Based on a rational decomposition of the amide I spectra, the structural conformation of dragline silk proteins and the proportion of those secondary structure were determined. This analysis shows that spider dragline silk containsβ-sheet,β-turn,α-helix and un-ordered structure elements;however, the proportions in which these structures appear changes with the spinning method. Theβ-sheet content of silk fiber obtained by artificial reeling at 20 mm/s is higher than that of spider spun fibers, indicating that some of the α-helix and other structures are transformed into β-sheet during the spider’s spinning process.