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University of Illinois at Urbana-Champaign

NMR Investigations of Structure in Pressure and Cold Denatured Proteins

Abstract

dc:description

Because of the extreme temperatures and pressures used to perform the cold denaturation studies, hydrogen exchange rates in model amides were measured at various temperatures and pressures to determine the effect of the extreme conditions. These reaction rates are compared to those obtained by correcting extant data for temperature and pressure.

Degree

thesis:*
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 and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Nash, David P.
Contributors dc:contributor
  • Jonas, Jiri

Subjects

dc:subject × 1

Rights

Language dc:language
eng

Identifiers

dc:identifier.*
Identifier
(MiAaPQ)AAI9834720
OAI identifier oai:identifier
oai:www.ideals.illinois.edu:2142/84400

Chain of custody

source
Harvested from
University of Illinois - Urbana-Champaign
Base URL
www.ideals.illinois.edu/oai-pmh
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Nash, David P.. NMR Investigations of Structure in Pressure and Cold Denatured Proteins. Dissertation thesis, University of Illinois at Urbana-Champaign, 2015. http://hdl.handle.net/2142/84400