Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/15163
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dc.titleProtein complex studies on calmodulin - GAP-43 (neuromodulin)
dc.contributor.authorLIU BO
dc.date.accessioned2010-04-08T10:50:40Z
dc.date.available2010-04-08T10:50:40Z
dc.date.issued2005-12-28
dc.identifier.citationLIU BO (2005-12-28). Protein complex studies on calmodulin - GAP-43 (neuromodulin). ScholarBank@NUS Repository.
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/15163
dc.description.abstractCalmodulin (CaM) is a ubiquitous Ca2+-binding protein found in all eukaryotic cells. It interacts with a wide variety of proteins and modulates their functions. In low intracellular Ca2+ concentration, Ca2+-free CaM (apoCaM) interacts with proteins containing IQ motif. GAP-43 (Neuromodulin) is a neuron specific growth-associated protein containing IQ-motif as its CaM-binding domain. It is considered to be a major determinant of synaptic development and plasticity, and has been implicated in molecular mechanisms underlying learning and memory. PKC phosphorylation has important effects on the interaction between CaM and GAP-43.CaM and a GAP-43 truncate (GAP-43t) were overexpressed and purified. Protein complex of apoCaM and GAP-43t was obtained by GTA crosslinking and identified by SDS-PAGE analysis. This protein complex provides a new approach to the studies on both the CaM a?? GAP-43 interaction and the apoCaM a?? IQ motif interaction. Further studies on the protein complex will provide significant insights into both interactions.
dc.language.isoen
dc.subjectprotein complex, Calmodulin, GAP-43, IQ motif, GTA, crosslinking
dc.typeThesis
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.contributor.supervisorSHEU FWU-SHAN
dc.contributor.supervisorJAYARAMAN SIVARAMAN
dc.description.degreeMaster's
dc.description.degreeconferredMASTER OF SCIENCE
dc.identifier.isiutNOT_IN_WOS
Appears in Collections:Master's Theses (Open)

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