Ribonuclease T1 has different dimensions in the thermally and chemically denatured states: a dynamic light scattering study.

Abstract Ribonuclease T1 can be unfolded and refolded without forming noticeable amounts of aggregates allowing to characterise the dimensions of a protein in different denatured states in terms of the Stokes radius R S . Upon thermal unfolding R S increases from 1.74 nm at 20°C to 2.14 nm at 60°C. By contrast, R S =2.40 nm was obtained at 5.3 M guanidinium chloride (GuHCl) and 20°C. Heating from 20°C to 70°C in the presence of 5.3 M GuHCl led to a 5% decrease in R S . © 1997 Federation of European Biochemical Societies.