The Role of Hydration in Protein Stability: Comparison of the Cold and Heat Unfolded States of Yfh1

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• 作者：Miquel Adrover¹ ; ² ; Gabriel Martorell³ ; Stephen R. Martin¹ ; Dunja Urosev⁴ ; Petr V. Konarev⁵ ; Dmitri I. Svergun⁵ ; Xavier Daura⁴ ; ⁶ ; Pierandrea Temussi¹ ; ⁷ ; Annalisa Pastore¹ ; ^{apastor@nimr.mrc.ac.uk}
• 关键词：SAXS ; small-angle X-ray scattering ; MD ; molecular dynamics ; HSQC ; heteronuclear single quantum coherence ; SSP ; secondary structure propensity ; EOM ; ensemble optimization method
• 刊名：Journal of Molecular Biology
• 出版年：2012
• 期刊代码：102_00222836
• 类别：imm
• 出版时间：13 April, 2012
• 卷：417
• 期：5
• 页码：413-424
• 文件大小：698 K

摘要

Protein unfolding occurs at both low and high temperatures, although in most cases, only the high-temperature transition can be experimentally studied. A pressing question is how much the low- and high-temperature denatured states, although thermodynamically equivalent, are structurally and kinetically similar. We have combined experimental and computational approaches to compare the high- and low-temperature unfolded states of Yfh1, a natural protein that, at physiologic pH, undergoes cold and heat denaturation around 0聽掳C and 40聽掳C without the help of ad hoc destabilization. We observe that the two denatured states have similar but not identical residual secondary structures, different kinetics and compactness and a remarkably different degree of hydration. We use molecular dynamics simulations to rationalize the role of solvation and its effect on protein stability.