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Title
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Secondary structure and hydrogen bonding of crambin in solution. A two-dimensional NMR study.
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Authors
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R.M.Lamerichs,
L.J.Berliner,
R.Boelens,
A.De Marco,
M.Llinàs,
R.Kaptein.
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Ref.
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Eur J Biochem, 1988,
171,
307-312.
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PubMed id
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Abstract
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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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