Secondary structure and hydrogen bonding of crambin in solution. A two-dimensional NMR study |
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Authors: | R M Lamerichs L J Berliner R Boelens A De Marco M Llinàs R Kaptein |
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Affiliation: | Department of Organic Chemistry, University of Utrecht, The Netherlands. |
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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. |
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