Protein structural transitions and their functional role

Philos Trans A Math Phys Eng Sci. 2005 Feb 15;363(1827):331-55; discussion 355-6. doi: 10.1098/rsta.2004.1496.

Abstract

Living cells are a collection of molecular machines which carry out many of the functions essential for the cell's existence, differentiation and reproduction. Most, though not all, of these machines are made up of proteins. Because of their complexity, an understanding of how they work requires a synergistic combination of experimental and theoretical studies. In this paper we outline our studies of two such protein machines. One is GroEL, the chaperone from Escherichia coli, which aids in protein folding; the other is F(1)-ATPase, a motor protein which synthesizes and hydrolyses ATP.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Chaperonin 60 / chemistry*
  • Chaperonin 60 / metabolism*
  • Energy Transfer / physiology*
  • Models, Biological*
  • Models, Chemical
  • Models, Molecular*
  • Molecular Motor Proteins / chemistry
  • Molecular Motor Proteins / physiology
  • Motion
  • Protein Conformation
  • Protein Folding
  • Proton-Translocating ATPases / chemistry*
  • Proton-Translocating ATPases / metabolism*
  • Structure-Activity Relationship

Substances

  • Chaperonin 60
  • Molecular Motor Proteins
  • Proton-Translocating ATPases