2000/01/01 by Tom Chou, Chou, Tom, Ken S. Kim +3
Biochemistry, Genetics and Molecular Biology · Physics and Astronomy · #Advanced Thermodynamics and Statistical Mechanics #Biomolecules (q-bio.BM) #FOS: Biological sciences #FOS: Physical sciences #Lipid Membrane Structure and Behavior #Protein Structure and Dynamics #Soft Condensed Matter (cond-mat.soft) #Statistical Mechanics (cond-mat.stat-mech) #cond-mat.soft #cond-mat.stat-mech #q-bio.BM
paper · pdf · doi:10.48550/arxiv.cond-mat/0001001
22pp, 7 .eps figures, apalike.sty, submitted to Biophys. J
arxiv created 2000/01/01 · openalex publication_date 2000/01/01 · arxiv updated 2009/11/30 · openalex created_date 2019/06/27 · openalex updated_date 2026/07/28
Integral membrane proteins deform the surrounding bilayer creating long-ranged forces that influence distant proteins. These forces can be attractive or repulsive, depending on the proteins' shape, height, contact angle with the bilayer, as well as the local membrane curvature. Although interaction energies are not pairwise additive, for sufficiently low protein density, thermodynamic properties depend only upon pair interactions. Here, we compute pair interaction potentials and entropic contributions to the two-dimensional osmotic pressure of a collection of noncircular proteins. In contrast to direct short-ranged interactions such as van der Waal's, hydrophobic, or electrostatic interactions, both local membrane Gaussian curvature and protein ellipticity can induce attractions between two proteins at distances of up to ten times their typical radii. For flat membranes, bending rigidities of ∼ 30kBT, and moderate ellipticities, we find thermally averaged attractive interactions of order ∼ 2kBT. These interactions may play an important role in the intermediate stages of protein aggregation.