Enthalpically driven peptide stabilization by protective osmolytes

被引：100
|
作者：
Politi, Regina
Harries, Daniel [1 ]
机构：
[1] Hebrew Univ Jerusalem, Inst Chem, IL-91904 Jerusalem, Israel
来源：
CHEMICAL COMMUNICATIONS | 2010年 / 46卷 / 35期
基金：
以色列科学基金会;
关键词：
BETA-HAIRPIN PEPTIDE; PROTEIN STABILITY; WEAK-INTERACTIONS; WATER; HYDRATION; SOLUTES; EQUILIBRIA; INTERFACES; ENERGETICS; STRESS;
D O I：
10.1039/c0cc01763a
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
We determined the added enthalpic and entropic contributions of protective osmolytes to the folding of a model peptide into its native beta-hairpin state. In contrast to entropically driven steric "crowding", this study shows that sugars and polyols can act as protective osmolytes by primarily diminishing the unfavourable enthalpic contribution to folding.
引用
收藏
页码：6449 / 6451
页数：3
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