Functional protein domains from the thermally driven motion of polypeptide chains: A proposal
✍ Scribed by Jan H. Hoh
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 91 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0887-3585
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✦ Synopsis
It is proposed that the thermally driven motion of certain polypeptide chains, including those that are part of an otherwise stable folded protein, produces timeaveraged three-dimensional domains that confer unique functions to a protein. These domains may be controlled by collapsing the polypeptide into an enthalpically favored structure, or extending it into an entropically dominated form. In the extended form, these domains occupy a relatively large space, which may be used to regulate protein-protein interactions and confer mechanical properties to proteins. This ''entropic bristle'' model makes several predictions about the structure and properties of these domains, and the predictions are used to reevaluate a range of biophysical studies on proteins. The outcome of the analysis suggests that the entropic bristle can be used to explain a wide range of disparate and apparently unrelated experimental observations. Proteins 32: