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dc.contributor.authorTowse, Clare-Louise*
dc.contributor.authorHopping, G.G.*
dc.contributor.authorVulovic, I.M.*
dc.contributor.authorDaggett, V.*
dc.date.accessioned2017-03-06T13:36:29Z
dc.date.available2017-03-06T13:36:29Z
dc.date.issued2014-11-27
dc.identifier.citationTowse C, Hopping G, Vulovic IM et al (2014) Nature versus design: the conformational propensities of D-amino acids and the importance of side chain chirality. Protein Engineering Design and Selection. 27(11): 447-455.en_US
dc.identifier.urihttp://hdl.handle.net/10454/11547
dc.descriptionNoen_US
dc.description.abstractD-amino acids are useful building blocks for de novo peptide design and they play a role in aging-related diseases associated with gradual protein racemization. For amino acids with achiral side chains, one should be able to presume that the conformational propensities of L- and D-amino acids are a reflection of one another due to the straightforward geometric inversion at the Cα atom. However, this presumption does not account for the directionality of the backbone dipole and the inverted propensities have never been definitively confirmed in this context. Furthermore, there is little known of how alternative side chain chirality affects the backbone conformations of isoleucine and threonine. Using a GGXGG host-guest pentapeptide system, we have completed exhaustive sampling of the conformational propensities of the D-amino acids, including D-allo-isoleucine and D-allo-threonine, using atomistic molecular dynamics simulations. Comparison of these simulations with the same systems hosting the cognate L-amino acids verifies that the intrinsic backbone conformational propensities of the D-amino acids are the inverse of their cognate L-enantiomers. Where amino acids have a chiral center in their side chain (Thr, Ile) the β-configuration affects the backbone sampling, which in turn can confer different biological properties.en_US
dc.description.sponsorshipNIHen_US
dc.language.isoenen_US
dc.relation.isreferencedbyhttp://dx.doi.org/10.1093/protein/gzu037en_US
dc.subjectMD simulation; Conformational sampling; D-amino acids; Epimerisation; Racemisationen_US
dc.titleNature versus design: the conformational propensities of D-amino acids and the importance of side chain chiralityen_US
dc.status.refereedYesen_US
dc.date.Accepted2014-08-11
dc.date.application2014-09-18
dc.typeArticleen_US
dc.type.versionNo full-text in the repositoryen_US


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