02001nas a2200205   4500008004100000022001400041245008200055210006900137260011000206300001400316490000700330520119600337100002401533700002501557700002501582700002601607700002601633700002001659856011601679       2015                        eng d  a1463-907600aThermodynamic and kinetic characterization of transmembrane helix association0 aThermodynamic and kinetic characterization of transmembrane heli  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcNOV  a1390-13980 v173 a<p>The transient dimerization of transmembrane proteins is an important event in several cellular processes and computational methods are being increasingly used to quantify their underlying energetics. Here, we probe the thermodynamics and kinetics of a simple transmembrane dimer to understand membrane protein association. A multi-step framework has been developed in which the dimerization profiles are calculated from coarse-grain molecular dynamics simulations, followed by meso-scale simulations using parameters calculated from the coarse-grain model. The calculated value of Delta G(assoc) is approx. -20 kJ mol(-1) and is consistent between three methods. Interestingly, the meso-scale stochastic model reveals low dimer percentages at physiologically-relevant concentrations, despite a favorable Delta G(assoc). We identify generic driving forces arising from the protein backbone and lipid bilayer and complementary factors, such as protein density, that govern self-interactions in membranes. Our results provide an important contribution in understanding membrane protein organization and linking molecular, nano-scale computational studies to meso-scale experimental data.</p>1 aPawar, Aiswarya, B.1 aDeshpande, Sneha, A.1 aGopal, Srinivasa, M.1 aWassenaar, Tsjerk, A.1 aAthale, Chaitanya, A.1 aSengupta, Durba  uhttps://library.ncl.res.in/content/thermodynamic-and-kinetic-characterization-transmembrane-helix-association-0