Applications of liquid state NMR spectroscopy for protein structure, dynamics, and folding, and for quantum computation.
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Applications of liquid state NMR spectroscopy for protein structure, dynamics, and folding, and for quantum computation. by Jason Edward Ollerenshaw

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Published .
Written in English


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The remarkable versatility of liquid state nuclear magnetic resonance spectroscopy has led to its ubiquitous application in chemical and biochemical research. This thesis describes three research projects united by the theme of liquid state NMR methodology.Improvements in spectrometer technology, isotopic labeling strategies, and pulse sequence design are continually extending the upper size limit for NMR studies of proteins. In the first part of this thesis, a series of experiments that take advantage of the unique spectroscopic properties of macromolecular methyl groups to collect well-resolved data from very large proteins with optimal sensitivity are described, and demonstrated on samples of an 81.4kDa enzyme. A theoretical analysis of each experiment, using single-transition spin operators to describe the evolution and relaxation of the ensemble during each stage of the experiment, is provided.Quantum computing promises spectacular advances in the speed with which certain calculations can be performed, but the theory has developed faster than the experimental reality. Modern NMR equipment and methods allow the researcher to control the evolution of an ensemble of quantum systems with precision unrivalled by any other technique, making NMR an ideal experimental testing ground for new theoretical concepts in quantum information processing. In the third part, an NMR-based experimental implementation of quantum computing is described in which a previously undemonstrated decoherence-free encoding is used to avoid errors during the execution of an algorithm in the presence of strong engineered noise.The goal of protein folding research is to determine how an unstructured polypeptide chain with thousands of degrees of freedom can rapidly find a very specific folded conformation determined by the molecule"s amino acid sequence. Protein folding is best studied using techniques such as NMR spectroscopy and computer simulation that report on the process from multiple spatially resolved sites within the molecule. In a recent study of two mutants of the Fyn SH3 domain, sparingly populated folding intermediates were identified and structurally characterized using relaxation dispersion NMR techniques. The second part of this thesis describes an extension of this study in which the same behaviour was identified in a simplified computational model of the wild-type protein.

The Physical Object
Pagination184 leaves.
Number of Pages184
ID Numbers
Open LibraryOL21302745M
ISBN 100494075902

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