1H‐NMR assignment and folding of the isolated ribonuclease 21–42 fragment
- 1 July 1988
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 175 (1) , 101-109
- https://doi.org/10.1111/j.1432-1033.1988.tb14171.x
Abstract
We show in this paper that the isolated bovine ribonuclease 21-42 fragment is able to adopt in water solution a measurable population (14% at 22 degrees C, pH 5.4) of a native-like alpha-helical structure. Strong support for this conclusion is given by the analysis of CD data and 1H chemical shift variations with the temperature and the addition of stabilizing (trifluoroethanol) and denaturing (urea) agents. This results gives experimental support to the idea that native isolated secondary structure elements (at least alpha helices) are, as a rule, partially stable in solution and therefore they can act as independent protein-folding nucleation centers.Keywords
This publication has 25 references indexed in Scilit:
- 1H NMR and CD evidence of the folding of the isolated ribonuclease 50–61 fragmentFEBS Letters, 1987
- Nuclear Overhauser effects in linear peptides A low‐temperature 500 MHz study of Met‐enkephalinFEBS Letters, 1987
- Conformational analyses of polyoxyethylene‐bound homo‐oligo‐L‐glutamates in a helix‐supporting environment, trifluoroethanolBiopolymers, 1985
- NH resonances of Ribonuclease S‐peptide in aqueous solution. Low temperature n.m.r. studyInternational Journal of Peptide and Protein Research, 1985
- Conformational dependence of the local nuclear overhauser effects in peptidesJournal of Magnetic Resonance (1969), 1984
- Low‐temperature 1H‐NMR evidence of the folding of isolated ribonuclease S‐peptideFEBS Letters, 1983
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983
- 1H n.m.r. parameters of the N‐terminal 19‐residue S‐peptide of ribonuclease in aqueous solutionInternational Journal of Peptide and Protein Research, 1983
- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OHBiopolymers, 1979
- Computed circular dichroism spectra for the evaluation of protein conformationBiochemistry, 1969