Title: Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case
Authors: Graña-Montes, Ricardo
de Groot, Natalia S
Castillo Cano, Virginia
Sancho, Javier
Velazquez-Campoy, Adrian
Ventura, Salvador # ×
Issue Date: Jan-2012
Publisher: Mary Ann Liebert, Inc.
Series Title: Antioxidants & Redox Signaling vol:16 issue:1 pages:1-15
Article number: 10.1089/ars.2011.3936
Abstract: The failure of proteins to fold or to remain folded very often leads to their deposition into amyloid fibrils and is the origin of a variety of human diseases. Accordingly, mutations that destabilize the native conformation are associated with pathological phenotypes in several protein models. Protein backbone cyclization by disulfide bond crosslinking strongly reduces the entropy of the unfolded state and, usually, increases protein stability. The effect of protein cyclization on the thermodynamic and kinetics of folding has been extensively studied, but little is know on its effect on aggregation reactions.
ISSN: 1523-0864
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Non-KU Leuven Association publications
× corresponding author
# (joint) last author

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