Structure of the pressure-assisted cold denatured state of ubiquitin.
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.
Nash
D P
DP
School of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, Illinois 61801, USA.
Jonas
J
J
D003080:Cold Temperature; D006859:Hydrogen / Q000737:chemistry; D011312:Pressure; D011489:Protein Denaturation; D014452:Ubiquitins / Q000737:chemistry*
D014452:Ubiquitins; D006859:Hydrogen