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Title:Multinuclear magnetic resonance studies of proteins
Author(s):Le, Hongbiao
Doctoral Committee Chair(s):Oldfield, Eric
Department / Program:Biology, Molecular
Chemistry, Biochemistry
Chemistry, Physical
Discipline:Biology, Molecular
Chemistry, Biochemistry
Chemistry, Physical
Degree Granting Institution:University of Illinois at Urbana-Champaign
Subject(s):Biology, Molecular
Chemistry, Biochemistry
Chemistry, Physical
Abstract:We have used a multinuclear approach to study proteins in the work described in this dissertation. We first studied fluorine labeled avian egg white lysozymes. Mutagenesis and other chemical modification methods were used to assign resonances from (4-F) Phe- and (4;F) Trp- hen egg white lysozyme. Next we used the fluorine labeled hen egg white lysozyme to probe the denaturing properties of hen egg white lysozyme in denaturants of guanidine chloride, trifluoroethanol, urea and under thermal conditions. Our study is not limited to the experimental approaches. We first discussed what was the main factor that contributed to the fluorine chemical shifts in proteins based on recent new results. Pros and cons for the competing theories of van der Waals interaction and electrostatic field are discussed. Work on chemical shifts in proteins was extended to $\sp{13}$C and $\sp{15}$N chemical shifts in proteins. Using quantum ab initio method, we refined and improved the reproduction of these chemical shifts from known protein structures. The chemical shifts from C$\sp\alpha,$ C$\sp\beta,$ C$\sp\prime$ and backbone amide $\sp{15}$N of various residues have been investigated. Means of making full use of these newly discovered chemical shift related structural information were explored. Direct and indirect incorporation of the chemical shifts into protein structural refinement were both used and their results extensively compared and analyzed in terms of their impact on the protein backbone variance, dihedral angle variance and the ability to back calculate those observed chemical shifts.
Issue Date:1996
Rights Information:Copyright 1996 Le, Hongbiao
Date Available in IDEALS:2011-05-07
Identifier in Online Catalog:AAI9625153
OCLC Identifier:(UMI)AAI9625153

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