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 degrees and 60 degrees 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...

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Published inBiochimica et biophysica acta Vol. 1340; no. 2; pp. 235 - 244
Main Authors Damaschun, H, Gast, K, Hahn, U, Kröber, R, Müller-Frohne, M, Zirwer, D, Damaschun, G
Format Journal Article
LanguageEnglish
Published Netherlands 18.07.1997
Subjects
Disulfides - chemistry
Escherichia coli - enzymology
Mathematics
Plasmids
Protein Conformation
Protein Denaturation
Ribonuclease T1 - biosynthesis
Ribonuclease T1 - chemistry
Ribonuclease T1 - isolation & purification
Temperature
X-Ray Diffraction
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Summary:Small-angle X-ray scattering of RNase T1 with intact disulfide bonds was measured at 20 degrees and 60 degrees 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 degrees 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.
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ISSN:0006-3002