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Ribonuclease T1 has different dimensions in the thermally and chemically denatured states: a dynamic light scattering
K Gast1, D Zirwer, H Damaschun
1Max-Delbrück-Center for Molecular Medicine Berlin-Buch, Germany. gast@orion.rz.mdc-berlin.de
FEBS Letters
|February 24, 1997
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 RS. Upon thermal unfolding RS increases from 1.74 nm at 20 degrees C to 2.14 nm at 60 degrees C. By contrast, RS = 2.40 nm was obtained at 5.3 M guanidinium chloride (GuHCl) and 20 degrees C. Heating from 20 degrees C to 70 degrees C in the presence of 5.3 M GuHCl led to a 5% decrease in RS.