Large scale ab initio modeling of structurally uncharacterized antimicrobial peptides reveals known and novel folds

• Main Authors: Kozic, M, Fox, S.J, Thomas, J.M, Verma, C.S, Rigden, D.J
• Other Authors: BIOLOGY (NU)
• Format: Article
• Published: John Wiley and Sons Inc. 2020
• Subjects: ceratotoxin D; CPF B1; garvicin A; histatin 2; ipomicin; kassinatuerin 1; latarcin 4a; lebocin peptide 1A; microcin M; odorranain M; polypeptide antibiotic agent; ponericin Q42; unclassified drug; amphibian protein; ant venom; antimicrobial cationic peptide; bacteriocin; disulfide; garvicin A, Lactococcus garvieae; histatin; HTN1 protein, human; kassinatuerin-1; peptide; ponericin-Q42, Ectatomma quadridens; ab initio calculation; alpha helix; amino acid sequence; Article; chemical interaction; disulfide bond; priority journal; protein folding; protein stability; protein structure; chemistry; human; molecular model; protein secondary structure; structure activity relation; Amino Acid Sequence; Amphibian Proteins; Ant Venoms; Antimicrobial Cationic Peptides; Bacteriocins; Disulfides; Histatins; Humans; Models, Molecular; Peptides; Protein Folding; Protein Stability; Protein Structure, Secondary; Structure-Activity Relationship
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/179040
• Institution: National University of Singapore

10.1002/prot.25473