A stopped-flow fluorescence study of the native and modified lysozyme |
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| Authors: | Khosrow Khalifeh Bijan Ranjbar Khosro Khajeh Hossein Naderi-Manesh Mehdi Sadeghi Sara Gharavi |
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| Institution: | (1) Department of Biophysics & Biochemistry, Faculty of Sciences, Tarbiat Modares University, P.O. Box, 14115-175, Tehran, Islamic Republic of Iran;(2) National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Islamic Republic of Iran;(3) Department of Biology, Faculty of Science, Al-Zahra University, Tehran, Islamic Republic of Iran |
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| 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. |
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| Keywords: | folding stopped-flow kinetics hen egg white lysozyme φ -value bioinformatics transition state |
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