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Updated: Aug 13, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
Structure of the pressure-assisted cold denatured state of ubiquitin
1School of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, Illinois 61801, USA.
Abstract:
The pressure-assisted cold denatured state of ubiquitin in aqueous solution was investigated by high resolution NMR. Hydrogen exchange kinetics were measured for backbone amide protons in the cold denatured protein to determine its structure. In contrast to cold denatured ribonuclease A and lysozyme, cold denatured ubiquitin shows little persistent secondary structure. The behavior of ubiquitin supports the idea of a relationship between the residual structure of pressure-assisted cold-denatured states and the structure of early folding intermediates provided they exist.
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