These researchers are studying the dynamic properties of a mutant of the Bovine Pancreatic Trypsin Inhibitor (BPTI) using nuclear magnetic resonance (NMR). BPTI is a model protein for studies of protein folding and thermodynamics. A greater understanding of the protein folding process is important for protein engineering and design, and possibly cures for diseases involving alterations of mis-folded proteins (e.g., b-amyloids and Alzheimers). The mutant of BPTI being investigated (G37A) has interesting thermodynamic and kinetic properties, including large destabilization (~5 kcal/mol) and a rollover of folding rates in a Chevron plot at low urea concentrations that is not present in the wild type protein. The large changes in the thermodynamic and kinetic properties of this mutant, which only adds a single methyl group to a glycine not in the core of the protein, is somewhat surprising. These researchers are determining the three-dimensional structure of BPTI-G37A by NMR to investigate the mechanism of altered properties of this mutant. In addition, they are measuring aromatic ring flip and amide hydrogen exchange rates to probe local dynamics. In order to achieve this work, these researchers are using computational resources at the Supercomputing Institute for processing and analysis of the NMR data as well as for molecular modeling calculations.
John Battiste, Research Associate
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URL: http://www.msi.umn.edu/about/publications/annualreport/ar2000/depts/Biochem_MolBio_BioPhys/woodward.html |
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