NDLI: Solvent isotope effects on the refolding kinetics of hen egg-white lysozyme.

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Solvent isotope effects on the refolding kinetics of hen egg-white lysozyme.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Itzhaki, L. S. Evans, P. A.
Description	Country affiliation: United kingdom Author Affiliation: Itzhaki LS ( Department of Biochemistry, University of Cambridge, United Kingdom.)
Abstract	Solvent isotope effects have been observed on the in vitro refolding kinetics of a protein, hen lysozyme. The rates of two distinct phases of refolding resolved by intrinsic fluorescence have been found to be altered, to differing extents, in D2O compared with H2O, and experiments have been conducted aimed at assessing the contributions to these effects from various possible sources. The rates were found to be essentially independent of whether backbone amide nitrogens were protiated or deuterated, indicating that making and breaking of their hydrogen bonding interactions is not associated with a substantial isotope effect. Neither were the rates significantly affected by adding moderate concentrations of sucrose or glycerol to the refolding buffer, suggesting that viscosity differences between H2O and D2O are also unlikely to explain the isotope effects. The data suggest that different factors, acting in opposing directions, may be dominant under different conditions. Thus, the isotope effect on the rate-determining step was found to be qualitatively reversed on going to low pH, suggesting that one component is probably associated with changes in the environments of carboxylate groups in forming the folding transition state. This term disappears at low pH as these groups are protonated and an opposing effect then dominates. It was not possible to identify this other effect on the basis of the present data, but a dependence of the hydrophobic interaction on solvent isotopic composition is a likely candidate.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	1
Volume Number	5
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1996-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Egg White Muramidase Chemistry Protein Folding Solvents Animals Hydrogen-ion Concentration Isotopes Kinetics Viscosity Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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Comparison of the kinetics of S-S bond, secondary structure, and active site formation during refolding of reduced denatured hen egg white lysozyme.

L-Arginine increases the solubility of unfolded species of hen egg white lysozyme.

A near-native state on the slow refolding pathway of hen lysozyme.

Solvent isotope effects on the refolding kinetics of hen egg-white lysozyme.

Molecular dynamics simulation of thionated hen egg white lysozyme.

Kinetic traps in lysozyme folding.

Crystallization and evaluation of hen egg-white lysozyme crystals for protein pH titration in the crystalline state.

Biophysical characterization of DNA and RNA aptamer interactions with hen egg lysozyme.

Evidence of two oxidation states of copper during aggregation of hen egg white lysozyme (HEWL).

Solvent isotope effects on the refolding kinetics of hen egg-white lysozyme.

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Comparison of the kinetics of S-S bond, secondary structure, and active site formation during refolding of reduced denatured hen egg white lysozyme.

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