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pubmed-article:3338468pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:3338468pubmed:dateRevised2007-7-23lld:pubmed
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pubmed-article:3338468pubmed:year1988lld:pubmed
pubmed-article:3338468pubmed:articleTitleSecondary structure and hydrogen bonding of crambin in solution. A two-dimensional NMR study.lld:pubmed
pubmed-article:3338468pubmed:affiliationDepartment of Organic Chemistry, University of Utrecht, The Netherlands.lld:pubmed
pubmed-article:3338468pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:3338468pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
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