Computational and NMR Investigations of Protein Structure

The research in this thesis represents an effort to better understand the structure of proteins, and to suggest new spectroscopic information which might be used to improve the resolution of such structures. Variations in spectroscopic observables are correlated with variations in the local geometry and electrostatic environment of proteins. The chemical nature of the interactions which govern both protein structure and function is also investigated. By comparing theory and experiment, the validity of calculated charge densities, rho( r), charge density topologies, ∂2rho/∂r irj, molecular dipole moments, mu, electrostatic potentials, phi( r), and electric field gradients, ∇E is established. These calculated properties are then used to investigate the nature of bonded and nonbonded interactions in proteins. In the culmination of this effort protein hydrogen bonds are described in terms of NMR spectroscopic observables and calculated electrostatic properties.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Arnold, William D.

Contributors dc:contributor

• Oldfield, Eric

• Chemistry, Physical

Language dc:language

eng

Identifier

(MiAaPQ)AAI9996610

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84504