title: Correlation of hydrogen exchange behaviour and thermal stability of lysozyme.
abstract: 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.
mesh_terms: D006859:Hydrogen; D007211:Indoles; D009682:Magnetic Resonance Spectroscopy; D009113:Muramidase; D011487:Protein Conformation; D013696:Temperature; D013816:Thermodynamics; D014364:Tryptophan
chemical_list: D007211:Indoles; D006859:Hydrogen; D014364:Tryptophan; D009113:Muramidase