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Folding and Structural Characterization of Highly Disulfide-Bonded Beetle Antifreeze Protein Produced in Bacteria

✍ Scribed by Yih-Cherng Liou; Margaret E Daley; Laurie A Graham; Cyril M Kay; Virginia K Walker; Brian D Sykes; Peter L Davies

Book ID: 115645637
Publisher: Elsevier Science
Year: 2000
Tongue: English
Weight: 154 KB
Volume: 19
Category: Article
ISSN: 1046-5928
DOI: 10.1006/prep.2000.1219

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## Abstract Disulfide bonds play a crucial role in the stabilization of the amphipathic folding of the diverse families of cysteine‐rich antimicrobial peptides. The determination of cysteine pairings in these peptides has largely depended on sequence homology criteria, since the classical methods o