Correlation of IR spectroscopic, heat capacity, diamagnetic susceptibility and enzymatic measurements on lysozyme powder

The interaction between protein and water is of fundamental importance for processes ranging from protein folding and enzymatic activity to anhydrobiosis. In this letter we bring together results from diverse types of measurements to give a unified picture of the hydration process for lysozyme. The...

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Bibliographic Details
Published inNature (London) Vol. 284; no. 5756; p. 572
Main Authors Careri, G, Gratton, E, Yang, P H, Rupley, J A
Format Journal Article
LanguageEnglish
Published England 10.04.1980
Subjects
Catalysis
Magnetics
Muramidase - metabolism
Protein Conformation
Spectrophotometry, Infrared
Structure-Activity Relationship
Thermodynamics
Water
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Summary:The interaction between protein and water is of fundamental importance for processes ranging from protein folding and enzymatic activity to anhydrobiosis. In this letter we bring together results from diverse types of measurements to give a unified picture of the hydration process for lysozyme. The data come principally from experiments with protein films and powders. The principal aim is to examine the relationship between the sites of water interaction, the extent of coverage, and the enzymatic activity, thus providing a better understanding of the relationship between water and enzyme dynamics.
ISSN:0028-0836
1476-4687
DOI:10.1038/284572a0