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A stopped-flow fluorescence study of the native and modified lysozyme

1Department of Biophysics & Biochemistry, Faculty of Sciences, Tarbiat Modares University, P.O. Box, 14115-175, Tehran, Islamic Republic of Iran

2National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Islamic Republic of Iran

3Department of Biology, Faculty of Science, Al-Zahra University, Tehran, Islamic Republic of Iran

© 2007 Institute of Molecular Biology, Slovak Academy of Sciences. This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License. (CC BY-NC-ND 3.0)

Citation Information: Biologia. Volume 62, Issue 3, Pages 258–264, ISSN (Online) 1336-9563, ISSN (Print) 0006-3088, DOI: 10.2478/s11756-007-0045-0, June 2007

Publication History

Published Online:
2007-06-01

Abstract

The protein folding kinetics of hen egg white lysozyme (HEWL) was studied using experimental and bioinformatics tools. The structure of the transition state in the unfolding pathway of lysozyme was determined with stopped-flow kinetics using intact HEWL and its chemically modified derivative, in which six lysine residues have been modified. The overall consistency of φ-value (φ ≈ 1) indicates that lysine side chains interactions are subject to breaking in the structure of the transition state. Following experimental evidences, multiple sequence alignment of lysozyme family in vertebrates and exact structural examination of lysozyme, showed that the α-helix in the structure of lysozyme has critical role in the unfolding kinetics.

Keywords: folding; stopped-flow kinetics; hen egg white lysozyme; φ-value; bioinformatics; transition state

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