Abstract
It is proposed that the thermally driven motion of certain polypeptide chains, including those that are part of an otherwise stable folded protein, produces time-averaged 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.
Original language | English (US) |
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Pages (from-to) | 223-228 |
Number of pages | 6 |
Journal | Proteins: Structure, Function and Genetics |
Volume | 32 |
Issue number | 2 |
DOIs | |
State | Published - Aug 1 1998 |
Keywords
- Glycosylation
- Molecular springs
- Phosphorylation
- Protein structure
- Protein-protein interactions
- Regulation
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Molecular Biology