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Influence of Protein Flexibility on the Electrostatic Energy Landscape in Gramicidin A

dc.contributor.authorCorry, Ben
dc.contributor.authorChung, Shin-Ho
dc.date.accessioned2015-12-13T22:58:46Z
dc.date.issued2005
dc.date.updated2015-12-12T07:24:15Z
dc.description.abstractWe describe an electrostatic model of the gramicidin A channel that allows protein atoms to move in response to the presence of a permeating ion. To do this, molecular dynamics simulations are carried out with a permeating ion at various positions within
dc.identifier.issn0175-7571
dc.identifier.urihttp://hdl.handle.net/1885/83451
dc.publisherSpringer
dc.sourceEuropean Biophysics Journal
dc.subjectKeywords: gramicidin A; ion channel; article; atom; calculation; conductance; electricity; energy; molecular dynamics; protein structure; simulation; statistical significance; Computer Simulation; Diffusion; Elasticity; Electrostatics; Energy Transfer; Gramicidin; Brownian dynamics; Conductance; Electrostatics; Gramicidin A; Ion channels; Ion permeation; Molecular dynamics; Protein motion; Simulation
dc.titleInfluence of Protein Flexibility on the Electrostatic Energy Landscape in Gramicidin A
dc.typeJournal article
local.bibliographicCitation.lastpage216
local.bibliographicCitation.startpage208
local.contributor.affiliationCorry, Ben, University of Western Australia
local.contributor.affiliationChung, Shin-Ho, College of Physical and Mathematical Sciences, ANU
local.contributor.authoruidChung, Shin-Ho, u8809509
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor029901 - Biological Physics
local.identifier.ariespublicationMigratedxPub11726
local.identifier.citationvolume34
local.identifier.doi10.1007/s00249-004-0442-z
local.identifier.scopusID2-s2.0-18844419188
local.type.statusPublished Version

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