Unfolding of ribonuclease A by guanidinium chloride. Protein internal motions studied by nuclear magnetic resonance spin-lattice relaxation in an off-resonance rotating frame
- 1 November 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 101 (23) , 7050-7055
- https://doi.org/10.1021/ja00517a045
Abstract
No abstract availableThis publication has 4 references indexed in Scilit:
- Hemoglobin aggregation in oxygenated sickle cells studied by carbon‐13 rotating frame spin–lattice relaxation in the presence of an off‐resonance radiofrequency fieldBiopolymers, 1979
- Protein rotational correlation times determined in aqueous solution by carbon-13 rotating frame spin-lattice relaxation in the presence of an off-resonance radiofrequency fieldJournal of the American Chemical Society, 1978
- Nuclear magnetic resonance evidence for a structural intermediate at an early stage in the refolding of ribonuclease AJournal of Molecular Biology, 1978
- The correlation of ribonuclease activity with specific aspects of tertiary structureBiochimica et Biophysica Acta, 1957