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dc.contributor.advisorBaker, Daviden_US
dc.contributor.authorRichter, Florianen_US
dc.date.accessioned2013-02-25T17:52:06Z
dc.date.available2014-02-26T12:08:08Z
dc.date.issued2013-02-25
dc.date.submitted2012en_US
dc.identifier.otherRichter_washington_0250E_10937.pdfen_US
dc.identifier.urihttp://hdl.handle.net/1773/21829
dc.descriptionThesis (Ph.D.)--University of Washington, 2012en_US
dc.description.abstractComputational protein design is a relatively new technique used to devise amino acid sequences to fold into proteins having novel structures or functions. Here, we first give an overview about the approaches and algorithms used in computational protein design, together with examples of recently reported successful designs of protein structure and function. Then we present in-detail a computational algorithm for one specific application of computational protein design, namely the de-novo design of catalytic activity. Next, we apply this algorithm to design catalysts for ester hydrolysis. Several low-activity catalysts were obtained, highlighting both the potential and the challenges inherent in computational design. Finally, we introduce another novel computational procedure for the de-novo design of protein backbones that make specific required interactions.en_US
dc.format.mimetypeapplication/pdfen_US
dc.language.isoen_USen_US
dc.rightsCopyright is held by the individual authors.en_US
dc.subjectcatalysis; computational protein design; enzyme design; hydrolysis; synthetic biologyen_US
dc.subject.otherBiochemistryen_US
dc.subject.otherChemistryen_US
dc.subject.otherBiological chemistryen_US
dc.titleComputational de-novo design of ester hydrolasesen_US
dc.typeThesisen_US
dc.embargo.termsRestrict to UW for 1 year -- then make Open Accessen_US


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