4.6 Article

ATP-induced noncooperative thermal unfolding of hen lysozyme

Journal

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.06.005

Keywords

Hen egg white lysozyme; Synchrotron radiation circular dichroism; Secondary structure; Noncooperative unfolding; Partially unfolded intermediate

Funding

  1. Chinese National Natural Science Foundation [10635060, 10725522]

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To understand the role of ATP underlying the enhanced amyloidosis of hen egg white lysozyme (HEWL), the synchrotron radiation circular dichroism, combined with tryptophan fluorescence, dynamic light-scattering, and differential scanning calorimetry, is used to examine the alterations of the conformation and thermal unfolding pathway of the HEWL in the presence of ATP, Mg2+-ATP, ADP, AMP, etc. It is revealed that the binding of ATP to HEWL through strong electrostatic interaction changes the secondary structures of HEWL and makes the exposed residue W62 move into hydrophobic environments. This alteration of W62 decreases the beta-domain stability of HEWL, induces a noncooperative unfolding of the secondary structures, and produces a partially unfolded intermediate. This intermediate containing relatively rich alpha-helix and less beta-sheet structures has a great tendency to aggregate. The results imply that the ease of aggregating of HEWL is related to the extent of denaturation of the amyloidogenic region, rather than the electrostatic neutralizing effect or monomeric beta-sheet enriched intermediate. (C) 2010 Elsevier Inc. All rights reserved.

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