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University of Illinois at Urbana-Champaign
NMR study of the unfolding of ribonuclease A, and dynamical studies of liquids in confined geometries
Abstract
dc:descriptionThe cold, heat, and pressure unfolding of RNase A has been studied by 1D and 2D $\sp1$H NMR spectroscopy, spin-lattice relaxation time measurements, and the pressure-jump hydrogen-exchange method. It was found that the pressure denatured states of RNase A display some characteristics of a molten globule, and all three α-helices and the β-sheet of the native protein remain partially folded structures in the pressure denatured state. $\sp1$H spectra of the denatured RNase A suggest that the cold and pressure denatured states are more structured than the heat denatured state, while the cold denatured state is more structured than the pressure denatured state.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Chemistry, Physical
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2011
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Zhang, Jing
- Contributors dc:contributor
-
- Jonas, Jiri
Subjects
dc:subject × 1Rights
dc:rights- Statement dc:rights
-
- Copyright 1994 Zhang, Jing
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
-
AAI9522193
(UMI)AAI9522193 - OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/23529