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 hydrogen bonds found i 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