Folding studies on ribonuclease A, a model protein
- 1 February 1997
- journal article
- review article
- Published by Elsevier in Folding and Design
- Vol. 2 (1) , R1-R11
- https://doi.org/10.1016/s1359-0278(97)00001-1
Abstract
No abstract availableKeywords
This publication has 65 references indexed in Scilit:
- Nature of the Unfolded State of Ribonuclease A: Effect of Cis−Trans X−Pro Peptide Bond IsomerizationBiochemistry, 1996
- Circular Dichroism Evidence for the Presence of Burst-Phase Intermediates on the Conformational Folding Pathway of Ribonuclease ABiochemistry, 1996
- Generation of a Non-prolyl cis Peptide Bond in Ribonuclease T1Journal of Molecular Biology, 1994
- Protein folding and stability: the pathway of folding of barnaseFEBS Letters, 1993
- High-resolution Three-dimensional Structure of Ribonuclease A in Solution by Nuclear Magnetic Resonance SpectroscopyJournal of Molecular Biology, 1993
- Local interactions favor the native 8-residue disulfide loop in the oxidation of a fragment corresponding to the sequence Ser-50-Met-79 derived from bovine pancreatic ribonuclease AProtein Journal, 1988
- 1H NMR and CD evidence of the folding of the isolated ribonuclease 50–61 fragmentFEBS Letters, 1987
- On the fundamental role of the glu 2−…Arg 10+ salt bridge in the folding of isolated ribonuclease a S-peptideBiochemical and Biophysical Research Communications, 1984
- Low‐temperature 1H‐NMR evidence of the folding of isolated ribonuclease S‐peptideFEBS Letters, 1983
- Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchangeJournal of Molecular Biology, 1979