Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/48373
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dc.contributor.authorZhu, Yien
dc.date.accessioned2012-04-09T01:39:48Zen
dc.date.available2012-04-09T01:39:48Zen
dc.date.copyright2012en
dc.date.issued2012en
dc.identifier.citationZhu, Y. (2012). Structural proteomics : elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprinting. Doctoral thesis, Nanyang Technological University, Singapore.en
dc.identifier.urihttps://hdl.handle.net/10356/48373en
dc.description.abstractWe have developed a in vivo hydroxyl radical protein footprinting method for investigating the structure-function relationship of three distinct yet common classes of membrane proteins, a porin protein (OmpF) involved in voltage gating, a heterodimer (integrin αLβ2) important in cell adhesion and signaling, and a receptor-ligand interaction (EGF-EGFR) of a typical receptor tyrosine kinase essential for cell growth and signaling. This work indicates that the hydroxyl radical footprinting technique is a promising approach to study the structural dynamics of the integral membrane proteins directly in the native environment on the cell surfaces, and furthermore, to understand the biological function of this important class of proteins that is challenging to be studied by other structural biological methods.en
dc.format.extent155 p.en
dc.language.isoenen
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleStructural proteomics : elucidating in vivo structural dynamics of integral membrane proteins by hydroxyl radical footprintingen
dc.typeThesisen
dc.contributor.supervisorSze Siu Kwanen
dc.contributor.schoolSchool of Biological Sciencesen
dc.description.degreeDOCTOR OF PHILOSOPHY (SBS)en
dc.identifier.doi10.32657/10356/48373en
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