Effect of ligand binding on the backbone dynamics of linear and circular constructs of SH3 Domain

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dc.contributor.advisorFushman, Daviden_US
dc.contributor.authorChhikara, Ishwar Singhen_US
dc.contributor.departmentBiochemistryen_US
dc.contributor.publisherDigital Repository at the University of Marylanden_US
dc.contributor.publisherUniversity of Maryland (College Park, Md.)en_US
dc.date.accessioned2005-02-02T06:52:33Z
dc.date.available2005-02-02T06:52:33Z
dc.date.issued2004-12-08en_US
dc.description.abstractPeptide backbone cyclization is an important bio-engineering tool that has been widely used to control the stability, structure and biological role of small peptides. Here we have analyzed the effect of ligand binding on the backbone dynamics of a linear and circular construct of N-terminal SH3 domain of the Murine C-Crk adapter protein. We have also determined the residues on the protein surface involved in binding with the ligand by carrying out a series of HSQC titration experiments at different (ligand/protein) concentrations. This is the first time that the interface for the adapter protein Murine c-Crk N-SH3 domain in complex with C3G derived peptide (ligand) in solution has been determined.en_US
dc.format.extent3328432 bytes
dc.format.mimetypeapplication/pdf
dc.identifier.urihttp://hdl.handle.net/1903/2140
dc.language.isoen_US
dc.subject.pqcontrolledChemistry, Biochemistryen_US
dc.titleEffect of ligand binding on the backbone dynamics of linear and circular constructs of SH3 Domainen_US
dc.typeThesisen_US

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