Dynamic Effects of Mutations in Eglin c Public Deposited

Downloadable Content

Download PDF
Last Modified
  • March 20, 2019
Creator
  • Clarkson, Michael
    • Affiliation: School of Medicine, Department of Biochemistry and Biophysics
Abstract
  • In order to investigate the mechanism of dynamic propagation in proteins and the role these responses play in energetic communication, a series of novel dynamic perturbationresponse experiments using NMR spin-relaxation of 15N and 2H were performed on the serine protease inhibitor eglin c. Although analysis was complicated in some cases by significant structural changes, a considerable number of mutations provoked a substantial response among contiguous side chains while leaving backbone dynamics unaltered. In contrast, some mutations induced dynamic effects that were distributed discontinuously through the protein and associated with very subtle structural changes. Side chains did not always produce reciprocal dynamic responses. Both the "contiguous network responses" and "disperse network responses" were associated with significant free energies of interaction. These results suggest that dynamic networks may play a role in energetic communication.
Date of publication
Keyword
DOI
Resource type
Rights statement
  • In Copyright
Advisor
  • Pielak, Gary J.
  • Lee, Andrew
Degree
  • Doctor of Philosophy
Degree granting institution
  • University of North Carolina at Chapel Hill Graduate School
Graduation year
  • 2006
Language
Parents:

This work has no parents.

Items