Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold

• Main Authors: Ivanov S.M., Cawley A., Huber R.G., Bond P.J., Warwicker J.
• Other Authors: BIOLOGY (NU)
• Format: Article
• Published: 2019
• Subjects: protein protein interaction; static electricity; alpha helix; amino acid sequence; bacterium; binding site; chemical phenomena; chemistry; conserved sequence; human; kinetics; metabolism; protein domain; sequence alignment; sequence homology; thermodynamics; amino acid; bacterial protein; bacterial toxin; DNA binding protein; DNA topoisomerase IV; membrane protein; parD protein, Bacteria; protein binding; ubiquitin conjugating enzyme; ubiquitin protein ligase; VapB protein, Bacteria; Amino Acid Sequence; Amino Acids; Bacteria; Bacterial Proteins; Bacterial Toxins; Binding Sites; Conserved Sequence; DNA Topoisomerase IV; DNA-Binding Proteins; Humans; Hydrophobic and Hydrophilic Interactions; Kinetics; Membrane Glycoproteins; Protein Binding; Protein Conformation, alpha-Helical; Protein Interaction Domains and Motifs; Sequence Alignment; Sequence Homology, Amino Acid; Static Electricity; Thermodynamics; Ubiquitin-Conjugating Enzymes; Ubiquitin-Protein Ligases
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/161171
• Institution: National University of Singapore

10.1371/journal.pone.0185928