Dynamic and kinetic investigations of SEM-5/SOS peptide interactions

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dc.contributor.advisorJose M. Barralen_US
dc.contributor.committeeMemberVincent J. Hilseren_US
dc.contributor.committeeMemberJuniji Iwaharaen_US
dc.creatorli chieh Chenen_US
dc.date.accessioned2011-12-20T16:04:34Z
dc.date.accessioned2014-02-19T22:05:03Z
dc.date.available2010-09-28en_US
dc.date.available2011-12-20T16:04:34Z
dc.date.available2014-02-19T22:05:03Z
dc.date.created2009-04-01en_US
dc.date.issued2009-04-01en_US
dc.description.abstractThe dynamics of SEM-5 SH3 domain protein can provide an important insight into how structural dynamics contribute to protein function. This is important because solving the structure of protein alone only provides the detail on the population weight average of native ensembles. NMR (Nuclear Magnetic Resonance) is one of the best techniques that can be used to elucidate the conformational fluctuation of SH3 domain under native condition, The hypothesis of this study is that the protein during ligand-free ¬form is undergoing an equilibrium between binding-competent (BC) and binding-incompetent (BI) states(1). In order to test this hypothesis, we apply a Glycine mutation in a solvent exposed and highly dynamic region within RT loop of SH3 domain protein. Through this mutation, we aim to manipulate the dynamics of the protein but preserve the protein-ligand interface. Several NMR methodologies including order parameter and line-shape analysis are applied to observe the correlation of protein dynamics with its function, taking into consideration several thermodynamic and kinetic aspects of the structural changes involved.\r\n\r\nen_US
dc.format.mediumelectronicen_US
dc.identifier.otheretd-04012009-154648en_US
dc.identifier.urihttp://hdl.handle.net/2152.3/85
dc.language.isoengen_US
dc.rightsCopyright © is held by the author. Presentation of this material on the TDL web site by The University of Texas Medical Branch at Galveston was made possible under a limited license grant from the author who has retained all copyrights in the works.en_US
dc.subjectSH3 domainproteinen_US
dc.subjectNMRen_US
dc.subjectline-shape analysisen_US
dc.subjectkineticsen_US
dc.titleDynamic and kinetic investigations of SEM-5/SOS peptide interactionsen_US
dc.type.genrethesisen_US
dc.type.materialtexten_US
thesis.degree.departmentHuman Biological Chemistry and Geneticsen_US
thesis.degree.grantorThe University of Texas Medical Branchen_US
thesis.degree.levelMasteren_US
thesis.degree.nameMaster of Scienceen_US

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