ArticleScientific reports2019
NMR structures and mutational analysis of the two peptides constituting the bacteriocin plantaricin S.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Article
- Thermophilin 13: In Silico Analysis Provides New Insight in Genes Involved in Bacteriocin Production.Microorganisms · 2023Article
- Review
- Zinc Binding to NAP-Type Neuroprotective Peptides: Nuclear Magnetic Resonance Studies and Molecular Modeling.Pharmaceuticals (Basel, Switzerland) · 2021Article
- The membrane topology of immunity proteins for the two-peptide bacteriocins carnobacteriocin XY, lactococcin G, and lactococcin MN shows structural diversity.MicrobiologyOpen · 2020Article
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2 authors.
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Abstract
The structure of the individual peptides of the two-peptide bacteriocin plantaricin S, an antimicrobial peptide produced by a Lactobacillus plantarum strain, has been determined in DPC micelles. The two peptides of plantaricin S, Pls-α and Pls-β, form an α-helix from and including residue 8 to 24 with a less structured region around residue 16-19 and an amphiphilic α-helix from and including residue 7 to 23, respectively. Activity assays on single amino acid-substituted GxxxG and GxxxG-like motifs show that substituting the Ser and Gly residues in the G
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