Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.656800
Title: EVV 2DIR : a novel approach for protein phosphorylation
Author: Cheung, Michelle
ISNI:       0000 0004 5349 5764
Awarding Body: Imperial College London
Current Institution: Imperial College London
Date of Award: 2014
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Abstract:
The novel Electron-Vibration-Vibration Two-Dimensional InfraRed (EVV 2DIR) technique is a nonlinear spectroscopic method that measures the vibrational coupling spectrum in a way analogous to the measurement of spin couplings by 2D NMR methods. To date, the main focus of this work has been on the development of EVV 2DIR as a tool for high-throughput, label-free protein identification and absolute quantification. One of the most promising areas where EVV 2DIR technique can provide complementary information not available via other established proteomic methods is for the study of post-translational modifications. This spectroscopy has demonstrated absolute quantification of phosphorylation levels in peptides, something difficult to achieve with other methods. The cyclin-dependent kinase inhibitor p27 is involved in orchestrating a variety of protein interactions in vivo that are key modulators of cell-cycle progression and that are often deregulated in cancer. The regulation of p27 is controlled by phosphorylation on serine, threonine and tyrosine residues thus providing a good model for EVV 2DIR studies.
Supervisor: Klug, David; Mann, David; Willison, Keith Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.656800  DOI: Not available
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