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Computational issues in protein nuclear magnetic resonance spectroscopy

Posted on:2006-11-13Degree:M.ScType:Thesis
University:University of Alberta (Canada)Candidate:Tu, XinFull Text:PDF
GTID:2454390008960229Subject:Biophysics
Abstract/Summary:
Nuclear Magnetic Resonance (NMR) Spectroscopy is one of a few current techniques which can be used to determine three-dimensional structures of biomolecules at atomic resolution. The operating principle of NMR is based on the nuclear magnetic resonance phenomenon of the atomic nucleus. While it has been widely used to determine conformation of biomolecules, NMR experimentation is extremely time-consuming for large molecules such as proteins, due to their structural complexity. Due to its popularity, innovative data analysis and computational methods have been applied in NMR Spectroscopy. The time needed to resolve protein structure using NMR can be dramatically decreased from years to weeks with the assistance of these innovative methods. This thesis provides a comprehensive survey of NMR Spectroscopy including the operating principle of nuclear magnetic resonance, the detailed procedure for protein structure determination by NMR Spectroscopy, a comprehensive review of existing methods used in NMR Spectroscopy, and the advantages of applying computational methods.
Keywords/Search Tags:Nuclear magnetic resonance, NMR, Spectroscopy, Computational, Used, Protein, Methods
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