title: Conformational trapping in a membrane environment: a regulatory mechanism for protein activity?
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 degrees 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.
authors.affiliation: Center for Interdisciplinary Magnetic Resonance at the National High Magnetic Field Laboratory, Institute of Molecular Biophysics, Florida State University, Tallahassee, 32306, USA.
authors.forename: S
authors.initials: S
authors.lastname: Arumugam
authors.forename: S
authors.initials: S
authors.lastname: Pascal
authors.forename: C L
authors.initials: CL
authors.lastname: North
authors.forename: W
authors.initials: W
authors.lastname: Hu
authors.forename: K C
authors.initials: KC
authors.lastname: Lee
authors.forename: M
authors.initials: M
authors.lastname: Cotten
authors.forename: R R
authors.initials: RR
authors.lastname: Ketchem
authors.forename: F
authors.initials: F
authors.lastname: Xu
authors.forename: M
authors.initials: M
authors.lastname: Brenneman
authors.forename: F
authors.initials: F
authors.lastname: Kovacs
authors.forename: F
authors.initials: F
authors.lastname: Tian
authors.forename: A
authors.initials: A
authors.lastname: Wang
authors.forename: S
authors.initials: S
authors.lastname: Huo
authors.forename: T A
authors.initials: TA
authors.lastname: Cross
mesh_terms: D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000502:physiology
chemical_list: D011506:Proteins