Folding of ribonuclease A from a partially disordered conformation. Kinetic study under transition conditions
- 1 May 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (11), 2470-2477
- https://doi.org/10.1021/bi00306a023
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 36 references indexed in Scilit:
- Electrophoretic analysis of the unfolding of proteins by ureaJournal of Molecular Biology, 1979
- On the computation of the tertiary structure of globular proteins IIJournal of Theoretical Biology, 1979
- Application of distance geometry to protein tertiary structure calculationsBiopolymers, 1979
- Immunochemical analysis of the conformational properties of intermediates trapped in the folding and unfolding of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1978
- On the computation of the tertiary structure of globular proteinsJournal of Theoretical Biology, 1978
- Nuclear magnetic resonance evidence for a structural intermediate at an early stage in the refolding of ribonuclease AJournal of Molecular Biology, 1978
- A folding model of α-lactalbumin deduced from the three-state denaturation mechanismJournal of Molecular Biology, 1977
- A quantitative treatment of the kinetics of the folding transition of ribonuclease ABiochemistry, 1976
- Conformation of ribonuclease S-peptideBiochemistry, 1968
- Some spectrophotometric and polarimetric experiments with ribonucleaseBiochimica et Biophysica Acta, 1957