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

10.1371/journal.pone.0185928

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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
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1611712024-04-03T10:34:48Z Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold Ivanov S.M. Cawley A. Huber R.G. Bond P.J. Warwicker J. BIOLOGY (NU) BIOLOGICAL SCIENCES 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 10.1371/journal.pone.0185928 PLoS ONE 12 10 e0185928 2019-11-01T07:48:14Z 2019-11-01T07:48:14Z 2017 Article Ivanov S.M., Cawley A., Huber R.G., Bond P.J., Warwicker J. (2017). Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold. PLoS ONE 12 (10) : e0185928. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0185928 19326203 https://scholarbank.nus.edu.sg/handle/10635/161171 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Unpaywall 20191101
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	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
spellingShingle	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 Ivanov S.M. Cawley A. Huber R.G. Bond P.J. Warwicker J. Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold
description	10.1371/journal.pone.0185928
author2	BIOLOGY (NU)
author_facet	BIOLOGY (NU) Ivanov S.M. Cawley A. Huber R.G. Bond P.J. Warwicker J.
format	Article
author	Ivanov S.M. Cawley A. Huber R.G. Bond P.J. Warwicker J.
author_sort	Ivanov S.M.
title	Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold
title_short	Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold
title_full	Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold
title_fullStr	Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold
title_full_unstemmed	Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold
title_sort	protein-protein interactions in paralogues: electrostatics modulates specificity on a conserved steric scaffold
publishDate	2019
url	https://scholarbank.nus.edu.sg/handle/10635/161171
_version_	1795374095462825984

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

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