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© Research
Publication : Journal of molecular biology

Correlation of hydrogen exchange behaviour and thermal stability of lysozyme

Team: Archived: Nuclear Magnetic Resonance Of Biomolecules
Member: Muriel Delepierre
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of molecular biology - 15 Aug 1983

Delepierre M, Dobson CM, Selvarajah S, Wedin RE, Poulsen FM

Link to Pubmed [PMID] – 6887252

J. Mol. Biol. 1983 Aug;168(3):687-92

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.