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