Ribonuclease T1 has different dimensions in the thermally and chemically denatured states: a dynamic light scattering study.
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.
Gast
K
K
Max-Delbrück-Center for Molecular Medicine Berlin-Buch, Germany. gast@orion.rz.mdc-berlin.de
Zirwer
D
D
Damaschun
H
H
Hahn
U
U
Müller-Frohne
M
M
Wirth
M
M
Damaschun
G
G
D004926:Escherichia coli / Q000201:enzymology; D019791:Guanidine; D006146:Guanidines; D006358:Hot Temperature; D008027:Light; D011489:Protein Denaturation; D006163:Ribonuclease T1 / Q000737:chemistry*; D012542:Scattering, Radiation
D006146:Guanidines; D006163:Ribonuclease T1; D019791:Guanidine