Rational design, conformational analysis and membrane-penetrating dynamics study of Bac2A-derived antimicrobial peptides against gram-positive clinical strains isolated from pyemia

DOI10.1016/J.JTBI.2019.03.018zbMath1414.92198OpenAlexW2936686723WikidataQ92656785 ScholiaQ92656785MaRDI QIDQ2419827

Xiaolu Bai, Xiao-Lin Chen

Publication date: 4 June 2019

Published in: Journal of Theoretical Biology (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1016/j.jtbi.2019.03.018

zbMATH Keywords

amphipathicityantimicrobial peptideBac2Agram-positive bacteriummembrane-penetrating dynamicspyemia

Mathematics Subject Classification ID

Biochemistry, molecular biology (92C40) Protein sequences, DNA sequences (92D20) Medical epidemiology (92C60)

Uses Software

• Gromacs
• Pse-in-One
• iDrug-Target
• iNuc-PhysChem
• iPhos-PseEvo
• pLoc-mEuk
• iRNAm5C-PseDNC
• pLoc-mGneg
• pLoc-mPlant
• pLoc_bal-mGpos
• HELIQUEST

Cites Work

• Some remarks on protein attribute prediction and pseudo amino acid composition
• SPrenylC-PseAAC: a sequence-based model developed via Chou's 5-steps rule and general PseAAC for identifying S-prenylation sites in proteins
• Self-binding peptides: binding-upon-folding \textit{versus} folding-upon-binding
• The disposition of the LZCC protein residues in wenxiang diagram provides new insights into the protein-protein interaction mechanism
• Gram-positive and Gram-negative protein subcellular localization by incorporating evolutionary-based descriptors into Chou's general PseAAC

This page was built for publication: Rational design, conformational analysis and membrane-penetrating dynamics study of Bac2A-derived antimicrobial peptides against gram-positive clinical strains isolated from pyemia