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dc.creatorBechert, Charles Johnen_US
dc.date.accessioned2013-02-22T20:40:01Z
dc.date.available2013-02-22T20:40:01Z
dc.date.created1999en_US
dc.date.issued2013-02-22
dc.identifier.urihttp://hdl.handle.net/1969.1/ETD-TAMU-1999-Fellows-Thesis-B434en_US
dc.descriptionDue to the character of the original source materials and the nature of batch digitization, quality control issues may be present in this document. Please report any quality issues you encounter to digital@library.tamu.edu, referencing the URI of the item.en_US
dc.descriptionIncludes bibliographical references (leaves 30-32).en_US
dc.description.abstractThe goal of this research was to determine how protein stability is affected when tyrosines form specific inter and/or intramolecular hydrogen bonds in the folded state. Our model protein, the enzyme RNase Sa, contains four Tyr residues believed to form one or more intermolecular hydrogen bonds to surface or partially buried water molecules. To study these interactions the single mutants Tyr 30, 49, 55, 81 ʾPhe were prepared and their conformational stability and thermodynamics of folding analyzed. From thermal denaturation data the free energy of unfolding, DGu, enthalpy of unfolding, DH, the melting temperature, Tm, and heat capacity change associated with unfolding, DCp, have been calculated. Initial analysis of Tyr 30, 49, 55, 81 predicted that each residue formed hydrogen bonds to one or more water molecules; however, thermodynamic and NMR data from this study support the surprising results that Tyr 81 actually makes an atypical intramolecular bond contributing 1.2 KcaI/mol to stability. Data for Tyr 30, 49, 55 support the prediction that intermolecular hydrogen bonds to water molecules are formed.en_US
dc.format.mediumelectronicen_US
dc.format.mimetypeapplication/pdfen_US
dc.language.isoen_USen_US
dc.publisherTexas A&M Universityen_US
dc.rightsThis thesis was part of a retrospective digitization project authorized by the Texas A&M University Libraries in 2008. Copyright remains vested with the author(s). It is the user's responsibility to secure permission from the copyright holder(s) for re-use of the work beyond the provision of Fair Use.en_US
dc.subjectchemistry.en_US
dc.subjectMajor chemistry.en_US
dc.titleThe contribution of tyrosine water=hydrogen bonds to protein stabilityen_US
thesis.degree.departmentchemistryen_US
thesis.degree.disciplinechemistryen_US
thesis.degree.nameFellows Thesisen_US
thesis.degree.levelUndergraduateen_US
dc.type.genrethesisen_US
dc.type.materialtexten_US
dc.format.digitalOriginreformatted digitalen_US


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