Functional protein domains from the thermally driven motion of polypeptide chains: a proposal.
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.
Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. jan.hoh@jhu.edu
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D000494:Allosteric Regulation; D001665:Binding Sites; D003460:Crystallization; D019277:Entropy; D004789:Enzyme Activation; D006031:Glycosylation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008956:Models, Chemical; D008970:Molecular Weight; D010455:Peptides / Q000737:chemistry*; D010766:Phosphorylation; D011487:Protein Conformation; D017510:Protein Folding; D013269:Stochastic Processes; D013329:Structure-Activity Relationship; D013696:Temperature
D010455:Peptides