Functional protein domains from the thermally driven motion of polypeptide chains: A proposal

Jan H. Hoh

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)223-228
Number of pages6
JournalProteins: Structure, Function and Genetics
Volume32
Issue number2
DOIs
StatePublished - Aug 1 1998

Keywords

  • Glycosylation
  • Molecular springs
  • Phosphorylation
  • Protein structure
  • Protein-protein interactions
  • Regulation

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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