Conformational trapping in a membrane environment: A regulatory mechanism for protein activity?

S. Arumugam, S. Pascal, C. L. North, W. Hu, K. C. Lee, M. Cotten, R. R. Ketchem, F. Xu, M. Brenneman, F. Kovacs, F. Tian, A. Wang, S. Huo, T. A. Cross

Research output: Contribution to journalArticlepeer-review

48 Scopus citations

Abstract

Functional regulation of proteins is central to living organisms. Here it is shown that a nonfunctional conformational state of a polypeptide can be kinetically trapped in a lipid bilayer environment. This state is a metastable structure that is stable for weeks just above the phase transition temperature of the lipid. When the samples are incubated for several days at 68°C, 50% of the trapped conformation converts to the minimum-energy functional state. This result suggests the possibility that another mechanism for functional regulation of protein activity may be available for membrane proteins: that cells may insert proteins into membranes in inactive states pending the biological demand for protein function.

Original languageEnglish (US)
Pages (from-to)5872-5876
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume93
Issue number12
DOIs
StatePublished - Jun 11 1996

Keywords

  • N solid-state NMR
  • membrane protein stability
  • membrane proteins
  • molecular memory
  • orientational constraints

ASJC Scopus subject areas

  • General

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