Conformational relaxations of urea- and guanidine hydrochloride-unfolded ferricytochrome c.
Open Access
- 1 December 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (24) , 8778-8780
- https://doi.org/10.1016/s0021-9258(17)38308-4
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme groupBiochemistry, 1976
- A quantitative treatment of the kinetics of the folding transition of ribonuclease ABiochemistry, 1976
- Protein-folding dynamicsNature, 1976
- Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residuesBiochemistry, 1975
- Laser Raman spectroscopy as a mechanistic probe of the phosphate transfer from adenosine triphosphate in a model systemBiochemistry, 1975
- Experimental and Theoretical Aspects of Protein FoldingAdvances in Protein Chemistry, 1975
- Comparison of predicted and experimentally determined secondary structure of adenyl kinaseNature, 1974
- Anisotropy effects in temperature-jump relaxation studies on solutions containing linear polymersJournal of the American Chemical Society, 1974
- Principles that Govern the Folding of Protein ChainsScience, 1973
- On the kinetics of the helix-coil transition of polypeptides in solutionJournal of Molecular Biology, 1965