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Title
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Sequential resonance assignment and secondary structure determination of the Ascaris trypsin inhibitor, a member of a novel class of proteinase inhibitors.
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Authors
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A.M.Gronenborn,
M.Nilges,
R.J.Peanasky,
G.M.Clore.
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Ref.
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Biochemistry, 1990,
29,
183-189.
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PubMed id
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Abstract
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The solution conformation of the Ascaris trypsin inhibitor, a member of a novel
class of proteinase inhibitors, has been investigated by nuclear magnetic
resonance spectroscopy. Complete sequence-specific assignments of the 1H NMR
spectrum have been obtained by using a number of two-dimensional techniques for
identifying through-bond and through-space (less than 5-A) connectivities.
Elements of regular secondary structure have been identified on the basis of a
qualitative interpretation of the nuclear Overhauser enhancement, coupling
constant, and amide exchange data. These are two beta-sheet regions. One
double-stranded antiparallel beta-sheet comprises residues 11-14 (strand 1) and
37-39 (strand 2). The other triple-stranded sheet is formed by two antiparallel
strands comprising residues 45-49 (strand 4) and 53-57 (strand 5) connected by a
turn (residues 50-52), and a small strand consisting of residues 20-22 (strand
3) that is parallel to strand 4.
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