Insertion and Assembly of Membrane Proteins via Simulation.

@article{citeulike:531757, abstract = {Interactions of lipids are central to the folding and stability of membrane proteins. Coarse-grained molecular dynamics simulations have been used to reveal the mechanisms of self-assembly of protein/membrane and protein/detergent complexes for representatives of two classes of membrane protein, namely, glycophorin (a simple alpha-helical bundle) and OmpA (a beta-barrel). The accuracy of the coarse-grained simulations is established via comparison with the equivalent atomistic simulations of self-assembly of protein/detergent micelles. The simulation of OmpA/bilayer self-assembly reveals how a folded outer membrane protein can be inserted in a bilayer. The glycophorin/bilayer simulation supports the two-state model of membrane folding, in which transmembrane helix insertion precedes dimer self-assembly within a bilayer. The simulations also suggest that a dynamic equilibrium exists between the glycophorin helix monomer and dimer within a bilayer. The simulated glycophorin helix dimer is remarkably close in structure to that revealed by NMR. Thus, coarse-grained methods may help to define mechanisms of membrane protein (re)folding and will prove suitable for simulation of larger scale dynamic rearrangements of biological membranes.}, address = {Contribution from the Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.}, author = {Bond, P. J. and Sansom, M. S. }, citeulike-article-id = {531757}, doi = {http://dx.doi.org/10.1021/ja0569104}, issn = {0002-7863}, journal = {J Am Chem Soc}, keywords = {insertion, membrane, protein, protocol}, month = {March}, number = {8}, pages = {2697--2704}, posted-at = {2006-03-06 16:07:30}, priority = {2}, title = {Insertion and Assembly of Membrane Proteins via Simulation.}, url = {http://dx.doi.org/10.1021/ja0569104}, volume = {128}, year = {2006} }

TY - JOUR ID - citeulike:531757 L3 - citeulike-article-id:531757 N2 - Interactions of lipids are central to the folding and stability of membrane proteins. Coarse-grained molecular dynamics simulations have been used to reveal the mechanisms of self-assembly of protein/membrane and protein/detergent complexes for representatives of two classes of membrane protein, namely, glycophorin (a simple alpha-helical bundle) and OmpA (a beta-barrel). The accuracy of the coarse-grained simulations is established via comparison with the equivalent atomistic simulations of self-assembly of protein/detergent micelles. The simulation of OmpA/bilayer self-assembly reveals how a folded outer membrane protein can be inserted in a bilayer. The glycophorin/bilayer simulation supports the two-state model of membrane folding, in which transmembrane helix insertion precedes dimer self-assembly within a bilayer. The simulations also suggest that a dynamic equilibrium exists between the glycophorin helix monomer and dimer within a bilayer. The simulated glycophorin helix dimer is remarkably close in structure to that revealed by NMR. Thus, coarse-grained methods may help to define mechanisms of membrane protein (re)folding and will prove suitable for simulation of larger scale dynamic rearrangements of biological membranes. IS - 8 JF - J Am Chem Soc SN - 0002-7863 AD - Contribution from the Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K. EP - 2704 TI - Insertion and Assembly of Membrane Proteins via Simulation. VL - 128 SP - 2697 KW - insertion KW - membrane KW - protein KW - protocol AU - Bond, PJ AU - Sansom, MS PY - 2006/03/01/ UR - http://dx.doi.org/10.1021/ja0569104 ER -