Conformation of thermally denatured RNase T1 with intact disulfide bonds: A study by small-angle X-ray scattering

Small-angle X-ray scattering of RNase T1 with intact disulfide bonds was measured at 20° and 60°C in order to get insight into the structural changes of the protein caused by thermal denaturation. The radius of gyration increases from R G=1.43 nm to R G=2.21 nm. The conformations of the molecules at...

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Bibliographic Details
Published in:Biochimica et biophysica acta, Protein structure and molecular enzymology Protein structure and molecular enzymology, 1997-07, Vol.1340 (2), p.235-244
Main Authors: Damaschun, Hilde, Gast, Klaus, Hahn, Ulrich, Kröber, Reinhard, Müller-Frohne, Marlies, Zirwer, Dietrich, Damaschun, Gregor
Format: Article
Language:English
Subjects:
Denaturation
Folding intermediate
Protein folding
Protein structure
Ribonuclease T1
X-ray scattering
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Summary:Small-angle X-ray scattering of RNase T1 with intact disulfide bonds was measured at 20° and 60°C in order to get insight into the structural changes of the protein caused by thermal denaturation. The radius of gyration increases from R G=1.43 nm to R G=2.21 nm. The conformations of the molecules at 60°C are similar to those of ring-shaped random walk chains. However, the molecules are more compact than one would expect under theta conditions due to attractive interactions between the chain segments. The volume needed for free rotation of the thermally unfolded protein molecules about any axis in solution is five times greater than in the native state whereas the hydrodynamic effective volume is increasing only two times.
ISSN:0167-4838
1879-2588
DOI:10.1016/S0167-4838(97)00047-2