Solvent effects on the structure, dynamics and activity of lysozyme.
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Date
1985-08
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Abstract
Kuntz and Kauzmann have argued that dehydrating a protein results in conformational
changes. In contrast, Rupley et al. have developed a hydration model which involves
no significant change in conformation; the onset of enzyme activity in hen egg-white lysozyme
at hydration values of about 0·2 g water/g protein they ascribe rather to a solvation effect.
Using a direct difference infra-red technique we can follow specific hydration events as water is
added to a dry protein. Conformational studies of lysozyme using laser Raman spectroscopy
indicate changes in conformation with hydration that are complete just before measurable
activity is found. Parallel nuclear magnetic resonance measurements of exchangeability of the
main chain amide hydrogens, as a function of hydration from near dryness, suggest a
hydration-related increase in conformational flexibility which occurs before-and is probably
necessary for–the Raman–detected conformational changes. Very recent inelastic neutron
scattering measurements provides direct evidence of a flexibility change induced by hydration,
which is apparently necessary before the enzyme can achieve adequate flexibility for it to begin
to function.
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Keywords
Protein hydration, protein structure, hydration of lysozyme, activity of lysozyme, solvent effects on lysozyme
Citation
J L Finney, Poole P L. Solvent effects on the structure, dynamics and activity of lysozyme. Journal of Biosciences. 1985 Aug; 8(1&2): 25-35.