Cis-trans isomerization of proline in the peptide (his 105-Val 124) of ribonuclease a containing the primary nucleation site
- 1 April 1983
- journal article
- Published by Springer Nature in Protein Journal
- Vol. 2 (2) , 131-146
- https://doi.org/10.1007/bf01025377
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Effect of proline residues on protein foldingJournal of Molecular Biology, 1981
- Folding of ribonuclease, S-protein, and des(121-124)-ribonuclease during glutathione oxidation of the reduced proteinsBiochemistry, 1980
- A model-building procedure with particular application to proteinsActa Crystallographica Section A, 1980
- Evidence for involvement of proline cis-trans isomerization in the slow unfolding reaction of RNase A.Proceedings of the National Academy of Sciences, 1980
- Location of the antigenic determinants of bovine pancreatic ribonucleaseBiochemistry, 1979
- The X‐Pro peptide bond as an nmr probe for conformational studies of flexible linear peptidesBiopolymers, 1976
- Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residuesBiochemistry, 1975
- Experimental and Theoretical Aspects of Protein FoldingAdvances in Protein Chemistry, 1975
- Chain reversals in proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- The Primary Structure of Porcine Pancreatic RibonucleaseJournal of Biological Chemistry, 1970