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dc.contributor.authorRoeder, Konstantinen
dc.contributor.authorWales, Daviden
dc.date.accessioned2018-10-22T06:53:59Z
dc.date.available2018-10-22T06:53:59Z
dc.date.issued2018-08en
dc.identifier.issn1549-9618
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/284190
dc.description.abstractMany of the most interesting rearrangements associated with function and dysfunction of biomolecules involve complex, highly non-linear pathways. Predicting these convoluted changes in structure is an important research challenge, since knowledge of key intermediate conformations at an atomic level of detail has the potential to inform the design of novel therapeutic strategies with enhanced specificity. The identification of kinetically relevant pathways can be strongly dependent on the construction of a physically relevant initial pathway between specified endpoints, avoiding artefacts such as chain crossings. In this contribution we describe an enhanced interpolation procedure to characterise initial pathways for complex rearrangements of a histone tail, α-helix to β-sheet conversion for amyloid-β 17−42 , and egfr kinase activation. Complete connected initial pathways with relatively low overall barriers are obtained in each case using an enhanced quasi-continuous interpolation scheme. This approach will help to extend the complexity and time scales accessible to computer simulation.
dc.format.mediumPrint-Electronicen
dc.languageengen
dc.publisherAmerican Chemical Society (ACS)
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectHumansen
dc.subjectPeptide Fragmentsen
dc.subjectHistonesen
dc.subjectProtein Conformationen
dc.subjectProtein Structure, Secondaryen
dc.subjectAlgorithmsen
dc.subjectModels, Molecularen
dc.subjectComputer Simulationen
dc.subjectAmyloid beta-Peptidesen
dc.subjectErbB Receptorsen
dc.titlePredicting Pathways between Distant Configurations for Biomolecules.en
dc.typeArticle
prism.endingPage4278
prism.issueIdentifier8en
prism.publicationDate2018en
prism.publicationNameJournal of chemical theory and computationen
prism.startingPage4271
prism.volume14en
dc.identifier.doi10.17863/CAM.31558
dcterms.dateAccepted2018-07-02en
rioxxterms.versionofrecord10.1021/acs.jctc.8b00370en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2018-08en
dc.contributor.orcidRöder, Konstantin [0000-0003-2021-9504]
dc.contributor.orcidWales, David [0000-0002-3555-6645]
dc.identifier.eissn1549-9626
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idEPSRC (1652488)
pubs.funder-project-idEPSRC (EP/N035003/1)


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International