Denatured states of ribonuclease A have compact dimensions and residual secondary structure

Using small-angle X-ray scattering and Fourier transform infrared spectroscopy, we have determined that the thermally denatured state of native ribonuclease A is on average a compact structure having residual secondary structure. Under strongly reducing conditions, the protein further unfolds into a...

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Bibliographic Details
Published in:Biochemistry (Easton) 1992-09, Vol.31 (35), p.8329-8335
Main Authors: Sosnick, T. R, Trewhella, J
Format: Article
Language:English
Subjects:
Animals
Cattle
denaturation
Fourier Analysis
I.R. spectroscopy
Kinetics
pancreatic ribonuclease
Protein Conformation
Protein Denaturation
Ribonuclease, Pancreatic - chemistry
secondary structure
Spectrophotometry, Infrared
Thermodynamics
X ray scattering
X-Ray Diffraction
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Summary:Using small-angle X-ray scattering and Fourier transform infrared spectroscopy, we have determined that the thermally denatured state of native ribonuclease A is on average a compact structure having residual secondary structure. Under strongly reducing conditions, the protein further unfolds into a looser structure with larger dimensions but still retains a comparable amount of secondary structure. The dimensions of the thermally and chemically denatured states of the reduced protein are different but both are more compact than is predicted for a random coil of the same length. These results demonstrate that thermal denaturation in ribonuclease A is not a simple two-state transition from a native to a completely disordered random coil state.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00150a029