Open AccessStructure, dynamics and kinetics of two-component Lantibiotic Lichenicidin
Author(s) -
Alejandra de Miguel,
Rafael TapiaRojo,
Tillmann Utesch,
María Andrea Mroginski
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0179962
Subject(s) - lantibiotics , molecular dynamics , component (thermodynamics) , markov chain , random coil , kinetics , computational biology , chemistry , physics , protein secondary structure , biology , computer science , genetics , biochemistry , computational chemistry , bacteriocin , thermodynamics , quantum mechanics , machine learning , bacteria
Two variants of the two-component Lantibiotic Lichenicidin, produced by the strains B . Licheniformis VK21 and I89 (Lchα/ Lchβ and Bliα/ Bliβ peptides, respectively) have been investigated by means of 2 μs-long all-atom molecular dynamics simulations combined with Markov State Models. This rigorous statistical analysis enabled to evaluate the dynamic and kinetic properties of the aforementioned systems which are not accessible via experimental techniques. The structural flexibility characteristic of these small peptides is understood by a delicate equilibrium between random coil, α-helices and β-sheet structures. The undergoing secondary structure transitions from an α-helix to a β-sheet observed for Lchα and Lchβ peptides, were not present in the Bliα component and provide new insights to understand their mechanism of action.