Date of Award

6-2003

Document Type

Union College Only

Degree Name

Bachelor of Science

Department

Chemistry

Language

English

Abstract

NMR is a powerful experimental technique which can be used to determine protein structures. Central to this process is conversion of peak volumes in the NOE data sets into distance constraints and then structural refinement against those constraints. In general, each solution structural analysis is initiated de novo. We are interested in the structural analysis of a series of hybrids derived from two parental proteins (rubredoxins from mesophilic bacterium Clostridium pasteurianum (Cp) and the hyperthermophilic archaeon Pyrococcus furiosus (Pf)). Near 1 A resolution X-ray structures of Cp and Pf rubredoxins are available to provide a basis for quantitative comparison of the NOE volumes for analogous 1H-1H pairs in a difference analysis. In this approach, the volume differences are used to drive the structure away from the initial parentally derived model.

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