关于类弹性蛋白合成多肽的光谱研究。
Spectroscopic studies on elastin-like synthetic polypeptides.
作者信息
Castiglione-Morelli A, Scopa A, Tamburro A M, Guantieri V
机构信息
Department of Chemistry, Università della Basilicata, Potenza, Italy.
出版信息
Int J Biol Macromol. 1990 Dec;12(6):363-8. doi: 10.1016/0141-8130(90)90044-b.
Spectroscopic studies on synthetic polypeptides containing the unit-X-G-G (X=V or L) are reported. The sequences, constituting either fragments or model of elastin, were shown to adopt type II beta-turns together with an ensemble of unordered conformations. Furthermore, it was found that the stability of the beta-turns was depending on the nature of the X residue, on the hydration of the chain and, in the case of the sequence G-V-G-G-L, was decreasing by increasing the length of the chain.
报道了对含有单元-X-G-G（X = V或L）的合成多肽的光谱研究。构成弹性蛋白片段或模型的序列显示出采用II型β-转角以及无序构象的集合。此外，发现β-转角的稳定性取决于X残基的性质、链的水合作用，并且对于序列G-V-G-G-L而言，会随着链长度的增加而降低。
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