糖基化
肽
灵活性(工程)
单糖
化学
计算生物学
生物化学
调节器
生物
基因
数学
统计
作者
Bianca Villavicencio,Rodrigo Ligabue‐Braun,Hugo Verli
标识
DOI:10.1021/acs.jcim.1c01001
摘要
Glycocins are antimicrobial peptides with glycosylations, often an S-linked monosaccharide. Their recent structure elucidation has brought forth questions about their mechanisms of action as well as the impact of S-glycosylation on their structural behavior. Here, we investigated structural characteristics of glycocins using a computational approach. Depending on the peptide's class (sublancin- or glycocin F-like), the sugar changes the peptide's flexibility. Also, the presence of glycosylation is necessary for the lack of structure of Asm1. The C-terminal tail in glycocin F-like peptides influenced their structured regions, acting like a regulator. These findings corroborate the versatility of these post-translational modifications, pointing toward their potential use in molecular engineering.
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