Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/43663
Title: STRUCTURAL BASIS FOR THE REGULATION OF VOLTAGE GATED SODIUM CHANNELS BY CALMODULIN AND THE DEVELOPMENT OF LINKER METHODOLOGY TO TRAP THE TRANSIENT PROTEIN-PROTEIN INTERACTIONS
Authors: VISHNU PRIYANKA REDDY CHICHILI
Keywords: Calmodulin,Voltage Gated Sodium Channels,Linkers,protein-protein interactions,X-ray crystallography,inactivation kinetics
Issue Date: 24-Jan-2013
Source: VISHNU PRIYANKA REDDY CHICHILI (2013-01-24). STRUCTURAL BASIS FOR THE REGULATION OF VOLTAGE GATED SODIUM CHANNELS BY CALMODULIN AND THE DEVELOPMENT OF LINKER METHODOLOGY TO TRAP THE TRANSIENT PROTEIN-PROTEIN INTERACTIONS. ScholarBank@NUS Repository.
Abstract: Voltage gated sodium channels (VGSCs) play an important role in propagating action potentials. Calmodulin (CaM) is known to modulate the inactivation kinetics of VGSCs by interacting with their IQ motif. However, determining these protein-protein interactions at molecular level was a challenging task since these interactions are difficult to trap for structural studies. Towards, our objective we have thoroughly analyzed the presence and usage of Gly rich linkers in trapping various protein-protein/peptide interactions for structural studies. Based on our analysis, we have developed a method to trap protein complexes for structural studies using Gly rich linkers. Subsequently we have applied this method to trap CaM and NaV1.4/NaV1.6 IQ motif complexes for structural and functional studies. We have further validated these findings using in vitro and in vivo functional studies using full-length unlinked proteins. This study revealed the molecular basis for the isoform specific regulation of inactivation kinetics of VGSCs by CaM
URI: http://scholarbank.nus.edu.sg/handle/10635/43663
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