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Title:Rational Design of Chemotherapeutic Agents by Quantitative Structure-Activity Relationships and Solution NMR Methods for High Resolution Protein Structure Refinement
Author(s):Szabo, Christina Miki
Doctoral Committee Chair(s):Oldfield, Eric
Department / Program:Chemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Subject(s):Biophysics, General
Abstract:Second, work towards the study of solution protein structure refinement methods by high-resolution multi-dimensional nuclear magnetic resonance (NMR) spectroscopy is discussed. Uniformly 13C, 15N-labeled Saccharomyces cerevisiae iso-1 cytochrome c was overexpressed in Escherichia coli and purified in its ferric form for NMR studies. The chemical shifts of most of the 1H, 13C, and 15N nuclei were assigned for future analyses of the incorporation of 13Calpha chemical shift, 13Calpha chemical shift anisotropy, and residual dipolar coupling in the structure refinement calculation. The ultimate goal is the determination of a refinement method that includes the most effective combination of the types of restraints that will yield the most highly resolved protein structures. This will then have applications to structure-based methods of drug design, which rely upon the structure of the target enzyme and will complement the ligand-based method referred to above.
Issue Date:2001
Description:171 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2001.
Other Identifier(s):(MiAaPQ)AAI3030482
Date Available in IDEALS:2015-09-25
Date Deposited:2001

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