Hydration of denatured and molten globule proteins

被引：194

作者：

Denisov V.P. ^{[1
]}

Jonsson B.-H. ^{[2
]}

Halle B. ^{[1
]}

机构：

[1] Condensed Matter Magnetic Reson. G., Department of Chemistry, Lund University

[2] Department of Biochemistry, Umeå University

来源：

Nature Structural Biology | 1999年 / 6卷 / 3期

关键词：

D O I：

10.1038/6692

中图分类号：

学科分类号：

摘要：

The hydration of nonnative states is central to protein folding and stability but has been probed mainly by indirect methods. Here we use water 17O relaxation dispersion to monitor directly the internal and external hydration of α-lactalbumin, lysozyme, ribonuclease A, apomyoglobin and carbonic anhydrase in native and nonnative states. The results show that nonnative proteins are more structured and less solvent exposed than commonly believed. Molten globule proteins preserve most of the native internal hydration sites and have native-like surface hydration. Proteins denatured by guanidinium chloride are not fully solvent exposed but contain strongly perturbed occluded water. These findings shed new light on hydrophobic stabilization of proteins.

引用

页码：253 / 260

页数：7

共 14 条

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