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dc.contributor.authorKim, Taehoon
dc.contributor.authorLee, Kyu, II
dc.contributor.authorMorris, Phillip
dc.contributor.authorPastor, Richard W.
dc.contributor.authorAndersen, Olaf S.
dc.contributor.authorIm, Wonpil
dc.date.accessioned2015-04-22T19:59:23Z
dc.date.available2015-04-22T19:59:23Z
dc.date.issued2012-04-04
dc.identifier.citationKim, Taehoon, Kyu Il Lee, Phillip Morris, Richard W. Pastor, Olaf S. Andersen, and Wonpil Im. "Influence of Hydrophobic Mismatch on Structures and Dynamics of Gramicidin A and Lipid Bilayers." Biophysical Journal 102.7 (2012): 1551-560. http://dx.doi.org/10.1016/j.bpj.2012.03.014.en_US
dc.identifier.urihttp://hdl.handle.net/1808/17479
dc.descriptionThis is the publisher's version. Copyright 2012 by Elsevier.en_US
dc.description.abstractGramicidin A (gA) is a 15-amino-acid antibiotic peptide with an alternating L-D sequence, which forms (dimeric) bilayer-spanning, monovalent cation channels in biological membranes and synthetic bilayers. We performed molecular dynamics simulations of gA dimers and monomers in all-atom, explicit dilauroylphosphatidylcholine (DLPC), dimyristoylphosphatidylcholine (DMPC), dioleoylphosphatidylcholine (DOPC), and 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) bilayers. The variation in acyl chain length among these different phospholipids provides a way to alter gA-bilayer interactions by varying the bilayer hydrophobic thickness, and to determine the influence of hydrophobic mismatch on the structure and dynamics of both gA channels (and monomeric subunits) and the host bilayers. The simulations show that the channel structure varied little with changes in hydrophobic mismatch, and that the lipid bilayer adapts to the bilayer-spanning channel to minimize the exposure of hydrophobic residues. The bilayer thickness, however, did not vary monotonically as a function of radial distance from the channel. In all simulations, there was an initial decrease in thickness within 4–5 Å from the channel, which was followed by an increase in DOPC and POPC or a further decrease in DLPC and DMPC bilayers. The bilayer thickness varied little in the monomer simulations—except one of three independent simulations for DMPC and all three DLPC simulations, where the bilayer thinned to allow a single subunit to form a bilayer-spanning water-permeable pore. The radial dependence of local lipid area and bilayer compressibility is also nonmonotonic in the first shell around gA dimers due to gA-phospholipid interactions and the hydrophobic mismatch. Order parameters, acyl chain dynamics, and diffusion constants also differ between the lipids in the first shell and the bulk. The lipid behaviors in the first shell around gA dimers are more complex than predicted from a simple mismatch model, which has implications for understanding the energetics of membrane protein-lipid interactions.en_US
dc.publisherElsevieren_US
dc.titleInfluence of Hydrophobic Mismatch on Structures and Dynamics of Gramicidin A and Lipid Bilayersen_US
dc.typeArticle
kusw.kuauthorKim, Taehoon
kusw.kuauthorLee, Kyu II
kusw.kuauthorIm, Wonpil
kusw.kudepartmentMolecular Biosciencesen_US
kusw.kudepartmentCenter for Bioinformaticsen_US
dc.identifier.doi10.1016/j.bpj.2012.03.014
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item meets KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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