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- W330057143 abstract "Sapecin is a 40-residue peptide containing 6 half-cystine residues. The disulfide structure of sapecin was determined by sequencing cystine-containing peptides obtained by digesting sapecin with thermolysin. Results showed that sapecin has a vortical structure fixed by 3 disulfide bonds between cysteine residues 3 and 30, 16 and 36, and 20 and 38, respectively, and that these disulfide bonds are essential for its antibacterial activity." @default.
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- W330057143 date "1990-04-01" @default.
- W330057143 modified "2023-09-30" @default.
- W330057143 title "Determination of the Disulfide Array in Sapecin, an Antibacterial Peptide of Sarcophaga peregrina (Flesh Fly)1" @default.
- W330057143 cites W1907637398 @default.
- W330057143 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a123077" @default.
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