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

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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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Abbreviations

HEWL:

hen egg white lysozyme

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Authors and Affiliations

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

    Khosrow Khalifeh, Bijan Ranjbar, Khosro Khajeh & Hossein Naderi-Manesh

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

    Mehdi Sadeghi

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

    Sara Gharavi

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  1. Khosrow Khalifeh
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  2. Bijan Ranjbar
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  3. Khosro Khajeh
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  4. Hossein Naderi-Manesh
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  5. Mehdi Sadeghi
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  6. Sara Gharavi
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Correspondence to Bijan Ranjbar.

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Khalifeh, K., Ranjbar, B., Khajeh, K. et al. A stopped-flow fluorescence study of the native and modified lysozyme. Biologia 62, 258–264 (2007). https://doi.org/10.2478/s11756-007-0045-0

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