Energetics of hydrogen bonds in peptides.

Abstract:

:Hydrogen bonds and their relative strengths in proteins are of importance for understanding protein structure and protein motions. The correct strength of such hydrogen bonds is experimentally known to vary greatly from approximately 5-6 kcal/mol for the isolated bond to approximately 0.5-1.5 kcal/mol for proteins in solution. To estimate these bond strengths, here we suggest a direct novel kinetic procedure. This analyzes the timing of the trajectories of a properly averaged dynamic ensemble. Here we study the observed rupture of these hydrogen bonds in a molecular dynamics calculation as an alternative to using thermodynamics. This calculation is performed for the isolated system and contrasted with results for water. We find that the activation energy for the rupture of the hydrogen bond in a beta-sheet under isolated conditions is 4.76 kcal/mol, and the activation energy is 1.58 kcal/mol for the same beta-sheet in water. These results are in excellent agreement with observations and suggest that such a direct calculation can be useful for the prediction of hydrogen bond strengths in various environments of interest.

authors

Sheu SY,Yang DY,Selzle HL,Schlag EW

doi

10.1073/pnas.2133366100

keywords:

subject

Has Abstract

pub_date

2003-10-28 00:00:00

pages

12683-7

issue

22

eissn

0027-8424

issn

1091-6490

pii

2133366100

journal_volume

100

pub_type

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