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Paper   IPM / Biological / 13312
School of Biological Sciences
  Title:   A stopped-flow fluorescence study of the native and modified lysozyme
  Author(s): 
1.  K. Khalifeh.
2.  B. Ranjbar.
3.  K. Khajeh.
4.  H. Naderi-Manesh.
5.  M. Sadeghi.
6.  S. Gharavi.
  Status:   Published
  Journal: Biologia
  No.:  3
  Vol.:  62
  Year:  2007
  Pages:   258-264
  Supported by:  IPM
  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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