Anders Irbäck
Professor
Coupled folding-binding versus docking: A lattice model study
Author
Summary, in English
Using a simple hydrophobic/polar protein model, we perform a Monte Carlo study of the thermodynamics and kinetics of binding to a target structure for two closely related sequences, one of which has a unique folded state while the other is unstructured. We obtain significant differences in their binding behavior. The stable sequence has rigid docking as its preferred binding mode, while the unstructured chain tends to first attach to the target and then fold. The free-energy profiles associated with these two binding modes are compared. (C) 2004 American Institute of Physics.
Department/s
- Computational Biology and Biological Physics - Undergoing reorganization
Publishing year
2004
Language
English
Pages
3983-3989
Publication/Series
Journal of Chemical Physics
Volume
120
Issue
8
Document type
Journal article
Publisher
American Institute of Physics (AIP)
Topic
- Biophysics
Status
Published
ISBN/ISSN/Other
- ISSN: 0021-9606