Rare fluctuations of native proteins sampled by equilibrium hydrogen exchange

J Am Chem Soc. 2003 Dec 24;125(51):15686-7. doi: 10.1021/ja036523z.

Abstract

We present a method for determining the ensembles of native protein structures that result from the large fluctuations of low probability revealed by hydrogen-exchange experiments. The measured protection factors are used to bias Monte Carlo simulations to sample the structures of the exchange competent species. The approach is illustrated by its application to the case of alpha-lactalbumin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Humans
  • Hydrogen / chemistry*
  • Hydrogen / metabolism
  • Hydrogen Bonding
  • Kinetics
  • Lactalbumin / chemistry
  • Lactalbumin / metabolism
  • Models, Chemical
  • Monte Carlo Method
  • Protein Structure, Secondary
  • Proteins / chemistry*
  • Proteins / metabolism

Substances

  • Proteins
  • Hydrogen
  • Lactalbumin