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Title
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Assignment of the 1H nuclear magnetic resonance spectrum of the trypsin inhibitor homologue K from Dendroaspis polylepis polylepis. Two-dimensional nuclear magnetic resonance at 360 and 500 MHz.
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Authors
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R.M.Keller,
R.Baumann,
E.H.Hunziker-Kwik,
F.J.Joubert,
K.Wüthrich.
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Ref.
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J Mol Biol, 1983,
163,
623-646.
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PubMed id
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Abstract
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The assignment of the 1H nuclear magnetic resonance (n.m.r.) spectrum of the
trypsin inhibitor homologue K from the venom of Dendroaspis polylepis polylepis
is described and documented. The assignments are based entirely on the amino
acid sequence and on 2-dimensional n.m.r. experiments at 360 and 500 M Hz.
Individual assignments were obtained for the backbone and C beta protons of all
57 residues of the inhibitor homologue K, with the exceptions of the N-terminal
amino group, the amide protons of Arg16, Gly37 and Gly40 and the C beta protons
of Arg16 and Pro19. The assignments for the non-labile protons of the amino acid
side-chains are complete, with the exception of Gln29, Glu49 and all the
proline, lysine and arginine residues. For Asn and Trp the labile side-chain
protons have also been assigned. The chemical shifts for the assigned resonances
are listed for an aqueous solution at 50 degrees C and pH 3.4.
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