title: Protein structural transitions and their functional role.
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.
authors.affiliation: Laboratoire de Chimie Biophysique, ISIS, Université Louis Pasteur, Strasbourg, France.
authors.forename: Martin
authors.initials: M
authors.lastname: Karplus
authors.forename: Yi Qin
authors.initials: YQ
authors.lastname: Gao
authors.forename: Jianpeng
authors.initials: J
authors.lastname: Ma
authors.forename: Arjan
authors.initials: A
authors.lastname: van der Vaart
authors.forename: Wei
authors.initials: W
authors.lastname: Yang
mesh_terms: D018834:Chaperonin 60 / Q000737:chemistry* / Q000378:metabolism*; D004735:Energy Transfer / Q000502:physiology*; D008954:Models, Biological; D008956:Models, Chemical; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000502:physiology; D009038:Motion; D011487:Protein Conformation; D017510:Protein Folding; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D018834:Chaperonin 60; D020409:Molecular Motor Proteins; D006180:Proton-Translocating ATPases