Correlation of hydrogen exchange behaviour and thermal stability of lysozyme

J Mol Biol. 1983 Aug 15;168(3):687-92. doi: 10.1016/s0022-2836(83)80309-x.


The solvent exchange rates of individual indole NH hydrogens of tryptophan residues of lysozyme have been measured, by using 1H nuclear magnetic resonance spectroscopy, as a function of temperature in the presence of urea and following chemical modification. The results have been interpreted in terms of a low activation energy process which is not dependent on the thermal stability of the protein, and a higher activation energy process that is directly correlated with the thermal stability. The significance of these observations for an understanding of the dynamics of the protein is discussed.

Publication types

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

MeSH terms

  • Hydrogen
  • Indoles
  • Magnetic Resonance Spectroscopy
  • Muramidase*
  • Protein Conformation
  • Temperature
  • Thermodynamics
  • Tryptophan


  • Indoles
  • Hydrogen
  • Tryptophan
  • Muramidase