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dc.contributor.authorVerma, Rajni
dc.contributor.authorMitchell-Koch, Katie R.
dc.date.accessioned2015-03-26T18:28:15Z
dc.date.available2015-03-26T18:28:15Z
dc.date.issued2014-08-10
dc.identifier.citationVerma, Rajni; Mitchell-Koch, Katie R. 2014. Conformational dynamics of E. coli YqhD oxidoreductase in the presence of substrates. Abstracts of Papers of the American Chemical Society, Volume: 248 Meeting Abstract: 519-PHYSen_US
dc.identifier.issn0065-7727
dc.identifier.otherWOS:000349167404234
dc.identifier.urihttp://hdl.handle.net/10057/11164
dc.descriptionPresented at the 248th National Meeting of the American Chemical Society (ACS), San Francisco, California on August 13, 2014.en_US
dc.description.abstractE. coli YqhD exhibits aldehyde reductase and alcohol dehydrogenase activity with a broad substrate range. It has applications in the production of valuable biorenewable fuels and chemicals, such as isobutanol and 1,3-propanediol. Hence, this enzyme is an ideal candidate for protein engineering studies. In this work, we shed light on the change of conformational dynamics of YqhD in the presence of different substrates. Molecular dynamics simulations of YqhD were performed in pure water and near experimental concentrations of alcohols and aldehydes as substrates. The study aims to enhance the knowledge about the effect of substrate-enzyme interactions on the overall dynamics of the enzyme, and how these dynamics influence substrate accessibility to the active site. The outcome of the study will enhance our basic understanding of the relationships among structure, dynamics and function within this class of enzyme. The results have possible application to guide the rational design of YqhD to enhance substrate specificity and facilitate transport to the active site.en_US
dc.language.isoen_USen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofseriesAbstracts of Papers of the American Chemical Society;248
dc.titleConformational dynamics of E. coli YqhD oxidoreductase in the presence of substratesen_US
dc.typeAbstracten_US
dc.rights.holderCopyright © 2015 American Chemical Society


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