Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 35, Issue 10, Pages 539-546Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2010.04.009
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Funding
- EU [FP6-518230]
- Hungarian National Science Foundation [OTKA K69105]
- National Cancer Institute, National Institutes of Health [HHSN261200800001E]
- NIH, National Cancer Institute, Center for Cancer Research
- NATIONAL CANCER INSTITUTE [ZIABC010440, ZIABC010441] Funding Source: NIH RePORTER
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Single molecule and NMR measurements of protein dynamics increasingly uncover the complexity of binding scenarios. Here, we describe an extended conformational selection model that embraces a repertoire of selection and adjustment processes. Induced fit can be viewed as a subset of this repertoire, whose contribution is affected by the bond types stabilizing the interaction and the differences between the interacting partners. We argue that protein segments whose dynamics are distinct from the rest of the protein ('discrete breathers') can govern conformational transitions and allosteric propagation that accompany binding processes and, as such, might be more sensitive to mutational events. Additionally, we highlight the dynamic complexity of binding scenarios as they relate to events such as aggregation and signalling, and the crowded cellular environment.
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