NMR study of the unfolding of ribonuclease A, and dynamical studies of liquids in confined geometries
type: CreativeWork
description: The 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 $\alpha$-helices and the $\beta$-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.
abstract: The 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 $\alpha$-helices and the $\beta$-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.
author: Zhang, Jing
language: eng
keywords: Chemistry, Physical
date published: 2011-05-07T14:17:35Z
date modified: 2026-07-22T22:25:22Z
provider: University of Illinois - Urbana-Champaign
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Illinois at Urbana-Champaign

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2142/23529