Protection of amide protons in folding intermediates of ribonuclease A measured by pH pulse exchange curves
- 1 March 1985
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 24 (7), 1689-1693
- https://doi.org/10.1021/bi00328a018
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 18 references indexed in Scilit:
- A Native‐Like Intermediate on the Ribonuclease A Folding PathwayEuropean Journal of Biochemistry, 1981
- Structural intermediates trapped during the folding of ribonuclease A by amide proton exchangeBiochemistry, 1980
- Role of proline isomerization in folding of ribonuclease A at low temperaturesProceedings of the National Academy of Sciences, 1979
- Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchangeJournal of Molecular Biology, 1979
- An experimental procedure for increasing the structural resolution of chemical hydrogen-exchange measurements on proteins: Application to ribonuclease S peptideJournal of Molecular Biology, 1979
- Labeling of proteins by reductive methylation using sodium cyanoborohydride.Journal of Biological Chemistry, 1979
- Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease AJournal of Molecular Biology, 1978
- A simple filtration assay for measuring hydrogen exchange kinetics of proteins: Application to peptide and ligand binding reactionsAnalytical Biochemistry, 1977
- Concentration-dependent hydrogen exchange kinetics of 3H-labeled S-peptide in ribonuclease SJournal of Molecular Biology, 1976
- Some spectrophotometric and polarimetric experiments with ribonucleaseBiochimica et Biophysica Acta, 1957