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Title
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Sequence-specific 1H NMR assignments and identification of slowly exchanging amide protons in murine epidermal growth factor.
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Authors
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G.T.Montelione,
K.Wüthrich,
H.A.Scheraga.
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Ref.
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Biochemistry, 1988,
27,
2235-2243.
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PubMed id
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Abstract
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Proton nuclear magnetic resonance (1H NMR) assignments for the murine epidermal
growth factor (mEGF) in aqueous solution were determined by using
two-dimensional NMR at pH 3.1 and 28 degrees C. The assignments are complete for
all backbone hydrogen atoms, with the exception of the N-terminal amino group,
and for 46 of the 53 side chains. Among the additional seven amino acid
residues, three have complete assignments for all but one side-chain proton, and
between two and four protons are missing for the remaining four residues. The
sequential assignments by nuclear Overhauser effect spectroscopy are consistent
with the chemically determined amino acid sequence. The NMR data show that the
conformations of both the Tyr3-Pro4 and Cys6-Pro7 peptide bonds are trans in the
predominant solution structure. Proton-deuterium exchange rate constants were
also measured for 13 slowly exchanging amide protons. The information presented
here has been used elsewhere to determine the three-dimensional structure of
mEGF in aqueous solution.
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