{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,17]],"date-time":"2026-04-17T06:27:38Z","timestamp":1776407258160,"version":"3.51.2"},"reference-count":58,"publisher":"Public Library of Science (PLoS)","issue":"10","license":[{"start":{"date-parts":[[2011,10,20]],"date-time":"2011-10-20T00:00:00Z","timestamp":1319068800000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.ploscompbiol.org"],"crossmark-restriction":false},"short-container-title":["PLoS Comput Biol"],"DOI":"10.1371\/journal.pcbi.1002204","type":"journal-article","created":{"date-parts":[[2011,10,20]],"date-time":"2011-10-20T21:07:51Z","timestamp":1319144871000},"page":"e1002204","update-policy":"https:\/\/doi.org\/10.1371\/journal.pcbi.corrections_policy","source":"Crossref","is-referenced-by-count":41,"title":["Transmembrane Helix Dynamics of Bacterial Chemoreceptors Supports a Piston Model of Signalling"],"prefix":"10.1371","volume":"7","author":[{"given":"Benjamin A.","family":"Hall","sequence":"first","affiliation":[]},{"given":"Judith P.","family":"Armitage","sequence":"additional","affiliation":[]},{"given":"Mark S. P.","family":"Sansom","sequence":"additional","affiliation":[]}],"member":"340","published-online":{"date-parts":[[2011,10,20]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1016\/j.str.2009.08.005","article-title":"The piston rises again.","volume":"17","author":"JJ Falke","year":"2009","journal-title":"Structure"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1006\/jmbi.1996.0507","article-title":"High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor.","volume":"262","author":"JI Yeh","year":"1996","journal-title":"J Mol Biol"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/23512","article-title":"Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor.","volume":"400","author":"KK Kim","year":"1999","journal-title":"Nature"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1016\/j.cell.2006.06.058","article-title":"The HAMP domain structure implies helix rotation in transmembrane signaling.","volume":"126","author":"M Hulko","year":"2006","journal-title":"Cell"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"13684","DOI":"10.1021\/bi701832b","article-title":"Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: A disulfide mapping study.","volume":"46","author":"KE Swain","year":"2007","journal-title":"Biochem"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"16555","DOI":"10.1073\/pnas.0806401105","article-title":"Role of HAMP domains in chemotaxis signaling by bacterial chemoreceptors.","volume":"105","author":"CM Khursigara","year":"2008","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"1719","DOI":"10.1038\/emboj.2011.77","article-title":"Lateral density of receptor arrays in the membrane plane influences sensitivity of the <italic>E. coli<\/italic> chemotaxis response.","volume":"30","author":"CM Khursigara","year":"2011","journal-title":"EMBO J"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"10104","DOI":"10.1073\/pnas.96.18.10104","article-title":"Heightened sensitivity of a lattice of membrane receptors.","volume":"96","author":"T Duke","year":"1999","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1038\/nature02406","article-title":"Functional interactions between receptors in bacterial chemotaxis.","volume":"428","author":"V Sourjik","year":"2004","journal-title":"Nature"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"6975","DOI":"10.1021\/bi900641c","article-title":"The core signaling proteins of bacterial chemotaxis assemble to form an ultrastable complex.","volume":"48","author":"AH Erbse","year":"2009","journal-title":"Biochem"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"3824","DOI":"10.1021\/bi100055m","article-title":"Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.","volume":"49","author":"J Bhatnagar","year":"2010","journal-title":"Biochem"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"9722","DOI":"10.1021\/bi00030a010","article-title":"Transmembrane signaling by the aspartate receptor: engineered disulfides reveal static regions of the subunit interface.","volume":"34","author":"SA Chervitz","year":"1995","journal-title":"Biochem"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1073\/pnas.93.6.2545","article-title":"Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.","volume":"93","author":"SA Chervitz","year":"1996","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/S0968-0004(00)01770-9","article-title":"Transmembrane signaling in bacterial chemoreceptors.","volume":"26","author":"JJ Falke","year":"2001","journal-title":"Trends Biochem Sci"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"1358","DOI":"10.1021\/bi0015109","article-title":"Site-directed solid-state NMR measurement of a ligand-induced conformational change in the serine bacterial chemoreceptor.","volume":"40","author":"OJ Murphy","year":"2001","journal-title":"Biochem"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1126\/science.285.5434.1751","article-title":"A piston model for transmembrane signaling of the aspartate receptor.","volume":"285","author":"KM Ottemann","year":"1999","journal-title":"Science"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"5416","DOI":"10.1073\/pnas.92.12.5416","article-title":"Identification of functionally important helical faces in transmembrane segments by scanning mutagenesis.","volume":"92","author":"GF Lee","year":"1995","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"11546","DOI":"10.1073\/pnas.93.21.11546","article-title":"Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo.","volume":"93","author":"AG Hughson","year":"1996","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"912","DOI":"10.1110\/ps.4640102","article-title":"Modeling the transmembrane domain of bacterial chemoreceptors.","volume":"11","author":"ML Peach","year":"2002","journal-title":"Protein Sci"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"4651","DOI":"10.1128\/jb.178.15.4651-4660.1996","article-title":"Mutational analysis of a transmembrane segment in a bacterial chemoreceptor.","volume":"178","author":"JW Baumgartner","year":"1996","journal-title":"J Bacteriol"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"20839","DOI":"10.1074\/jbc.274.30.20839","article-title":"Different membrane anchoring positions of tryptophan and lysine in synthetic transmembrane alpha-helical peptides.","volume":"274","author":"MRR de Planque","year":"1999","journal-title":"J Biol Chem"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"6521","DOI":"10.1021\/bi000073v","article-title":"Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins.","volume":"39","author":"A Ridder","year":"2000","journal-title":"Biochem"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/j.sbi.2006.06.007","article-title":"Peptides in lipid bilayers: the power of simple models.","volume":"16","author":"JA Killian","year":"2006","journal-title":"Curr Opin Struct Biol"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"31723","DOI":"10.1074\/jbc.M110.152470","article-title":"Charged or aromatic anchor residue dependence of transmembrane peptide tilt.","volume":"285","author":"VV Vostrikov","year":"2010","journal-title":"J Biol Chem"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"5803","DOI":"10.1021\/ja100598e","article-title":"Changes in transmembrane helix alignment by arginine residues revealed by solid-state NMR experiments and coarse-grained MD simulations.","volume":"132","author":"VV Vostrikov","year":"2010","journal-title":"J Amer Chem Soc"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"14713","DOI":"10.1021\/bi980809c","article-title":"The preference of tryptophan for membrane interfaces.","volume":"37","author":"WM Yau","year":"1998","journal-title":"Biochem"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/S0968-0004(00)01626-1","article-title":"How proteins adapt to a membrane-water interface.","volume":"25","author":"JA Killian","year":"2000","journal-title":"Trends Biochem Sci"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0005-2736(01)00299-1","article-title":"Amino acid distributions in integral membrane protein structures.","volume":"1512","author":"MB Ulmschneider","year":"2001","journal-title":"Biochim Biophys Acta"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1016\/j.str.2008.01.014","article-title":"Coarse-grained MD simulations of membrane protein-bilayer self-assembly.","volume":"16","author":"KA Scott","year":"2008","journal-title":"Structure"},{"key":"ref30","first-page":"1917Pos","article-title":"Interaction of WALP peptides with lipid bilayers: Molecular dynamics simulations.","volume":"78","author":"HI Petrache","year":"2000","journal-title":"Biophys J"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1016\/j.bpj.2010.05.039","article-title":"Interpretation of <sup>2<\/sup>H-NMR experiments on the orientation of the transmembrane helix WALP23 by computer simulations.","volume":"99","author":"L Monticelli","year":"2010","journal-title":"Biophys J"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1021\/jp908320b","article-title":"Interactions of phospholipid bilayers with several classes of amphiphilic \u03b1-helical peptides: insights from coarse-grained molecular dynamics simulations.","volume":"114","author":"P Gkeka","year":"2010","journal-title":"J Phys Chem B"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"3452","DOI":"10.1021\/ja909347x","article-title":"Mechanism and kinetics of peptide partitioning into membranes from all-atom simulations of thermostable peptides.","volume":"132","author":"MB Ulmschneider","year":"2010","journal-title":"J Amer Chem Soc"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"L60","DOI":"10.1016\/j.bpj.2010.03.043","article-title":"Peptide partitioning properties from direct insertion studies.","volume":"98","author":"MB Ulmschneider","year":"2010","journal-title":"Biophys J"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"7812","DOI":"10.1021\/jp071097f","article-title":"The MARTINI forcefield: coarse grained model for biomolecular simulations.","volume":"111","author":"SJ Marrink","year":"2007","journal-title":"J Phys Chem B"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1021\/ct700324x","article-title":"The MARTINI coarse grained force field: extension to proteins.","volume":"4","author":"L Monticelli","year":"2008","journal-title":"J Chem Theor Comp"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"2697","DOI":"10.1021\/ja0569104","article-title":"Insertion and assembly of membrane proteins via simulation.","volume":"128","author":"PJ Bond","year":"2006","journal-title":"J Amer Chem Soc"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/j.jsb.2006.10.004","article-title":"Coarse-grained molecular dynamics simulations of membrane proteins and peptides.","volume":"157","author":"PJ Bond","year":"2007","journal-title":"J Struct Biol"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"11321","DOI":"10.1021\/bi800642m","article-title":"Coarse-grained molecular dynamics simulations of the energetics of helix insertion into a lipid bilayer.","volume":"47","author":"PJ Bond","year":"2008","journal-title":"Biochem"},{"key":"ref40","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1009362108","article-title":"Lipid packing drives the segregation of transmembrane helices into disordered lipid domains in model membranes.","author":"LV Sch\u00e4fer","year":"2011"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1080\/09687680802446534","article-title":"CGDB: a database of membrane protein\/lipid interactions by coarse-grained molecular dynamics simulations.","volume":"25","author":"AP Chetwynd","year":"2008","journal-title":"Molec Memb Biol"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"1940","DOI":"10.1016\/j.bpj.2011.02.041","article-title":"Exploring peptide-membrane interactions with coarse grained MD simulations.","volume":"100","author":"BA Hall","year":"2011","journal-title":"Biophys J"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"1268","DOI":"10.1021\/bi048969d","article-title":"Tryptophan residues flanking the second transmembrane helix (TM2) set the signaling state of the Tar chemoreceptor.","volume":"44","author":"RR Draheim","year":"2005","journal-title":"Biochem"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"14655","DOI":"10.1021\/bi061259i","article-title":"Tuning a bacterial chemoreceptor with protein-membrane interactions.","volume":"45","author":"RR Draheim","year":"2006","journal-title":"Biochem"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"1763","DOI":"10.1021\/bi0360206","article-title":"Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor.","volume":"43","author":"AS Miller","year":"2004","journal-title":"Biochem"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1529\/biophysj.107.124206","article-title":"Role of tryptophan residues in gramicidin channel organization and function.","volume":"95","author":"A Chattopadhyay","year":"2008","journal-title":"Biophys J"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"2326","DOI":"10.1529\/biophysj.105.073395","article-title":"Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: A systematic investigation of hydrophobic mismatch.","volume":"90","author":"SK Kandasamy","year":"2006","journal-title":"Biophys J"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/S0014-5793(03)00475-7","article-title":"Snorkeling of lysine side chains in transmembrane helices: how easy can it get?","volume":"544","author":"E Strandberg","year":"2003","journal-title":"FEBS Lett"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1021\/bi0481242","article-title":"Influence of flanking residues on tilt and rotation angles of transmembrane peptides in lipid bilayers. A solid-state H-2 NMR study.","volume":"44","author":"S Ozdirekcan","year":"2005","journal-title":"Biochem"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"6608","DOI":"10.1021\/bi00143a035","article-title":"Fluorescence studies of the secondary structure and orientation of a model ion channel peptide in phospholipid vesicles.","volume":"31","author":"L Chung","year":"1992","journal-title":"Biochem"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"3457","DOI":"10.1021\/bi00178a001","article-title":"A single hydrophobic to hydrophobic substitution in the transmembrane domain impairs aspartate receptor function.","volume":"33","author":"CJ Jeffery","year":"1994","journal-title":"Biochem"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/j.sbi.2004.07.007","article-title":"Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs.","volume":"14","author":"A Senes","year":"2006","journal-title":"Curr Opin Struct Biol"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1093\/protein\/12.10.863","article-title":"The Escherichia coli aspartate receptor: sequence specificity of a transmembrane helix studied by hydrophobic-biased random mutagenesis.","volume":"12","author":"CJ Jeffery","year":"1999","journal-title":"Prot Engng"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"ra56, 51","DOI":"10.1126\/scisignal.2000547","article-title":"The single transmembrane domain of human tyrosine kinases encode self interactions.","volume":"2","author":"C Finger","year":"2009","journal-title":"Science Signal"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"6241","DOI":"10.1021\/bi060609y","article-title":"Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies.","volume":"45","author":"E Li","year":"2006","journal-title":"Biochem"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"7812","DOI":"10.1021\/jp071097f","article-title":"The MARTINI force field: coarse grained model for biomolecular simulations.","volume":"111","author":"S-J Marrink","year":"2007","journal-title":"J Phys Chem B"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/j.chemphyslip.2005.03.001","article-title":"Simulation of gel phase formation and melting in lipid bilayers using a coarse grained model.","volume":"135","author":"S-J Marrink","year":"2005","journal-title":"Chem Phys Lipids"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1007\/s008940100045","article-title":"GROMACS 3.0: a package for molecular simulation and trajectory analysis.","volume":"7","author":"E Lindahl","year":"2001","journal-title":"J Molec Model"}],"container-title":["PLoS Computational Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pcbi.1002204","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,6,10]],"date-time":"2023-06-10T16:49:14Z","timestamp":1686415754000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pcbi.1002204"}},"subtitle":[],"editor":[{"given":"James M.","family":"Briggs","sequence":"first","affiliation":[]}],"short-title":[],"issued":{"date-parts":[[2011,10,20]]},"references-count":58,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2011,10,20]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pcbi.1002204","relation":{},"ISSN":["1553-7358"],"issn-type":[{"value":"1553-7358","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,10,20]]}}}