Effects of H2O and D2O on polyproline II helical structure.
Effects of H2O and D2O on polyproline II helical structure.
复制标题
H2O 和 D2O 对聚脯氨酸 II 螺旋结构的影响。
DOI：
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发表时间：
2004
影响因子：
15
通讯作者：
T. Creamer
中科院分区：
文献类型：
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作者：
Brian W. Chellgren;T. Creamer
溶剂与多肽链的相互作用是控制蛋白质折叠和稳定性的主要因素之一。在生物相关系统中，这种溶剂通常是水。水在肽折叠中的作用的实验估计可以通过溶剂微扰实验获得。对 H2O 水最简单的干扰是其同位素 D2O 形式。已知形成 PII 螺旋的肽与 D2O 相对于 H2O 的溶剂化增加了它们采用 PII 构象的倾向。
The interaction of solvent with a polypeptide chain is one of the primary factors controlling protein folding and stability. In biologically relevant systems, this solvent is most often water. Experimental estimates of the role of water in peptide folding can be obtained from solvent perturbation experiments. The simplest perturbant for H2O water is its isotopic D2O form. The solvation of peptides known to form PII helices with D2O versus H2O increases their propensity to adopt the PII conformation.