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- W1982218194 abstract "The 1H and 13C spectra of four peptides, L-Phe-Val-Arg-pNA, D-Phe-Val-Arg-pNA, L-Phe-Pip-Arg-pNA and D-Phe-Pip-Arg-pNA (pNA = p-nitroaniline, Pip = pipecolic acid residue), have been examined, and deductions made about their conformation in solution. The D-Phe peptides, which are cleaved especially rapidly by thrombin in water, have structures (in deuterated DMSO) in which the aromatic ring of the D-Phe residue is folded back over the Val or Pip residue. This arrangement is not found in the L-Phe peptides. It is proposed that this feature (in which Phe could be situated near Val and near the Arg-Gly bond of the A alpha chain in the three-dimensional structure of fibrinogen) may be especially advantageous for binding to the enzyme." @default.
- W1982218194 created "2016-06-24" @default.
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- W1982218194 date "2009-01-12" @default.
- W1982218194 modified "2023-09-23" @default.
- W1982218194 title "1H AND 13C NUCLEAR MAGNETIC RESONANCE SPECTRA OF SOME PEPTIDES WITH FIBRINOGEN-LIKE REACTIVITY" @default.
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- W1982218194 doi "https://doi.org/10.1111/j.1399-3011.1979.tb01884.x" @default.
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