Chellgren Brian W, Creamer Trevor P
Center for Structural Biology, Department of Molecular and Cellular Biochemistry, University of Kentucky, 800 Rose Street, Lexington, KY 40536-0298, USA.
J Am Chem Soc. 2004 Nov 17;126(45):14734-5. doi: 10.1021/ja045425q.
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.
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。在生物相关体系中，这种溶剂通常是水。水在肽折叠中作用的实验估计可以从溶剂扰动实验中获得。对于H₂O水来说，最简单的扰动剂是其同位素D₂O形式。已知能形成PII螺旋的肽在D₂O和H₂O中的溶剂化作用会增加它们采用PII构象的倾向。
