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Biochemistry. 1992 Sep 8;31(35):8329-35.

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

Author information

1
Life Sciences Division, Los Alamos National Laboratory, New Mexico 87545.

Abstract

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.

PMID:
1525171
[Indexed for MEDLINE]

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