期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 107, 期 7, 页码 2746-2750出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0914727107
关键词
binding mechanism; disordered proteins; fast folding; protein folding
资金
- National Science Foundation (NSF) [PHY-082283]
- National Institutes of Health [P01GM071862]
- Kimmelman Center for Macromolecular Assemblies
- Federal German Ministry for Education and Research
Biomolecular folding and function are often coupled. During molecular recognition events, one of the binding partners may transiently or partially unfold, allowing more rapid access to a binding site. We describe a simple model for this fly-casting mechanism based on the capillarity approximation and polymer chain statistics. The model shows that fly casting is most effective when the protein unfolding barrier is small and the part of the chain which extends toward the target is relatively rigid. These features are often seen in known examples of fly casting in protein-DNA binding. Simulations of protein-DNA binding based on well-funneled native-topology models with electrostatic forces confirm the trends of the analytical theory.
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