Secondary structure and hydrogen bonding of crambin in solution A two‐dimensional NMR study
- 1 January 1988
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 171 (1-2) , 307-312
- https://doi.org/10.1111/j.1432-1033.1988.tb13791.x
Abstract
The secondary structure of crambin in solution has been determined using two‐dimensional NMR and is found to be essentially identical to that of the crystal structure. The H–D exchange of most amide protons can be accounted for in terms of the hydrogen bonds found in the X‐ray structure. Exceptions are the amide protons of Cys‐4 and Ser‐6, which exchange more slowly than expected, and of Asn‐46 for which the exchange is faster. These results might be explained by a slightly different conformation of the C‐terminal region of the protein in solution. The slow exchange of the amides of Cys‐32 and Glu‐23 might be due to aggregation involving an extremely hydrophobic part of the protein in solution.This publication has 17 references indexed in Scilit:
- Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambinBiochemistry, 1987
- An empirical examination of potential-energy minimization using the well-determined structure of the protein crambinJournal of the American Chemical Society, 1986
- Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin.Proceedings of the National Academy of Sciences, 1986
- A protein structure from nuclear magnetic resonance data: lac Repressor headpieceJournal of Molecular Biology, 1985
- An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solutionJournal of Molecular Biology, 1985
- Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambinProceedings of the National Academy of Sciences, 1984
- The theory and practice of distance geometryBulletin of Mathematical Biology, 1983
- Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphurNature, 1981
- Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteinsJournal of Molecular Biology, 1979
- A crystalline polypeptide from the seed of Crambe abyssinicaPhytochemistry, 1965