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 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Gast K,Zirwer D,Damaschun H,Hahn U,Müller-Frohne M,Wirth M,Damaschun G

doi

10.1016/s0014-5793(97)00058-6

subject

Has Abstract

pub_date

1997-02-24 00:00:00

pages

245-8

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)00058-6

journal_volume

403

pub_type

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