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 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.
D002384:Catalysis; D008280:Magnetics; D009113:Muramidase / Q000378:metabolism; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D014867:Water
D014867:Water; D009113:Muramidase