Dynamics and thermodynamics of hyperthermophilic proteins by hydrogen exchange

Methods Enzymol. 2001:334:342-50. doi: 10.1016/s0076-6879(01)34481-6.

Abstract

The naturally occurring hydrogen exchange of protein molecules can provide nonperturbing site-resolved measurements of protein stability and flexibility and changes therein. The measurement and understanding of these issues is especially pertinent to studies of thermophilic proteins. This chapter briefly reviews the considerations necessary for measuring hydrogen exchange and translating HX measurements into these detailed protein parameters.

Publication types

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

MeSH terms

  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / metabolism
  • Hydrogen / chemistry*
  • Models, Chemical
  • Protein Conformation
  • Protein Denaturation
  • Protein Folding
  • Thermodynamics*

Substances

  • Archaeal Proteins
  • Hydrogen