TY - JOUR
T1 - Intrinsic reaction-cycle time scale of Na+,K+-ATPase manifests itself in the lipid-protein interactions of non-equilibrium membranes
AU - Bouvrais, H.
AU - Cornelius, F.
AU - Ipsen, J.H.
AU - Mouritsen, O.G.
PY - 2012
Y1 - 2012
N2 - Interaction between integral membrane proteins and the lipid-bilayer component of biological membranes is expected to mutually influence the proteins and the membrane. We present quantitative evidence of a manifestation of the lipid–protein interactions in liposomal membranes, reconstituted with actively pumping Na+,K+-ATPase, in terms of nonequilibrium shape fluctuations that contain a relaxation time, τ, which is robust and independent of the specific fluctuation modes of the membrane. In the case of pumping Na+-ions, analysis of the flicker-noise temporal correlation spectrum of the liposomes leads to τ ≃ 0.5 s, comparing favorably with an intrinsic reaction-cycle time of about 0.4 s from enzymology.
AB - Interaction between integral membrane proteins and the lipid-bilayer component of biological membranes is expected to mutually influence the proteins and the membrane. We present quantitative evidence of a manifestation of the lipid–protein interactions in liposomal membranes, reconstituted with actively pumping Na+,K+-ATPase, in terms of nonequilibrium shape fluctuations that contain a relaxation time, τ, which is robust and independent of the specific fluctuation modes of the membrane. In the case of pumping Na+-ions, analysis of the flicker-noise temporal correlation spectrum of the liposomes leads to τ ≃ 0.5 s, comparing favorably with an intrinsic reaction-cycle time of about 0.4 s from enzymology.
U2 - 10.1073/pnas.1209909109
DO - 10.1073/pnas.1209909109
M3 - Journal article
SN - 0027-8424
VL - 109
SP - 18442
EP - 18446
JO - Proceedings of the National Academy of Sciences (PNAS)
JF - Proceedings of the National Academy of Sciences (PNAS)
IS - 45
ER -