Low‐temperature 1H‐NMR evidence of the folding of isolated ribonuclease S‐peptide
- 17 October 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 162 (2), 314-319
- https://doi.org/10.1016/0014-5793(83)80779-0
Abstract
The temperature (−7°C to 45°C, pH 5.4) and pH (0°C) dependence of 1H chemical shifts of ribonuclease S-peptide (5 mM, 1 M NaCl) has been measured at 360 MHz. The observed variations evidence the formation of a partial helical structure, involving the fragment Thr-3—Met-13. Two salt-bridges stabilize the helix: those formed by Glu-9−…His-12+ and Glu-2−…Arg-10+. The structural features deduced from the 1H-NMR at low temperature for the isolated S-peptide are compatible with the structure shown by the same molecule in the ribonuclease S crystal.Keywords
This publication has 11 references indexed in Scilit:
- 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
- Strategy for trapping intermediates in the folding of ribonuclease and for using 1H‐NMR to determine their structuresBiopolymers, 1983
- A competing salt-bridge suppresses helix formation by the isolated C-peptide carboxylate of ribonuclease AJournal of Molecular Biology, 1982
- Local secondary structure in ribonuclease A denatured by guanidine · HCl near 1 °CJournal of Molecular Biology, 1982
- A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A.Proceedings of the National Academy of Sciences, 1982
- Determination of the relaxation time of the helix–coil transition of poly(γ‐benzyl‐L‐glutamate) by the nmr techniqueBiopolymers, 1975
- Nuclear magnetic resonance of synthetic polypeptidesPublished by Walter de Gruyter GmbH ,1973
- Relation between structure and function in some partially synthetic ribonucleases S′. I. Kinetic determinationsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- Helix-coil transition of the isolated amino terminus of ribonucleaseBiochemistry, 1971
- Polypeptides. XLIV. Potent synthetic S-peptide antagonistsJournal of the American Chemical Society, 1970