Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2188289 | Journal of Molecular Biology | 2007 | 7 Pages |
Abstract
The dimensions of a denatured protein, fully reduced ribonuclease A (r-RNase A), have been measured using synchrotron-based small angle X-ray scattering. The radius of gyration, 34–35 Å, is unchanged from 0–6 M guanidinium chloride and from 20–90 °C at pH 2.5, and agrees with the known scaling behavior for a multitude of chemically denatured states. The polypeptide is behaving as a statistical coil in the non-interacting, high-temperature limit.
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Authors
Jaby Jacob, Robin S. Dothager, P. Thiyagarajan, Tobin R. Sosnick,