The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1.

Abstract:

: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 °C and 40 °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.

journal_name

J Mol Biol

authors

Adrover M,Martorell G,Martin SR,Urosev D,Konarev PV,Svergun DI,Daura X,Temussi P,Pastore A

doi

10.1016/j.jmb.2012.02.002

subject

Has Abstract

pub_date

2012-04-13 00:00:00

pages

413-24

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(12)00142-8

journal_volume

417

pub_type

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