Structure properties calculated for protein complexes formed by disordered proteins

Published: 21 June 2018| Version 1 | DOI: 10.17632/5x9n2nr2xm.1
Contributor:
Balint Meszaros

Description

Table S2. Structural parameter abbreviations: SSa: fraction of residues in helical conformation SSb: fraction of residues in extended conformation SSc: fraction of residues in coil conformation SASA/H: Hydrophobic fraction of solvent accessible surface area (SASA) SASA/P: Polar fraction of SASA INT/H: Hydrophobic fraction of interface area INT/P: Polar fraction of interface area BUR/H: Hydrophobic fraction of buried surface area BUR/P: Polar fraction of buried surface area INT/TOT: Interface area / (interface area+SASA) BUR/TOT: Buried surface area / (interface area+SASA) interHH: Fraction of atomic level intermolecular interactions between two hydrophobic atoms interHP: Fraction of atomic level intermolecular interactions between a hydrophobic and a polar atom interPP: Fraction of atomic level intermolecular interactions between two polar atoms interBB: Fraction of atomic level intermolecular interactions between two backbone atoms interBS: Fraction of atomic level intermolecular interactions between a backbone and a sidechain atom interSS: Fraction of atomic level intermolecular interactions between two sidechain atoms intraHH: Fraction of atomic level intramolecular interactions between two hydrophobic atoms intraHP: Fraction of atomic level intramolecular interactions between a hydrophobic and a polar atom intraPP: Fraction of atomic level intramolecular interactions between two polar atoms intraBB: Fraction of atomic level intramolecular interactions between two backbone atoms intraBS: Fraction of atomic level intramolecular interactions between a backbone and a sidechain atom intraSS: Fraction of atomic level intramolecular interactions between two sidechain atoms inter/intra: number of atomic level interchain interactions / number of atomic level intrachain interactions Etot/res: Sum of interchain and intrachain pairwise interaction energies / number of residues in chain Eint/Etot: Sum of interchain pairwise interaction energies / sum of interchain and intrachain pairwise interaction energies (maximized at 1). Calc. averages & correlations: Mean, Standard error and Relative standard error of normalized or proportional structural parameters in all groups and correlations between them. Grey background highlights those weakly correlation parameters that were selected for further calculations. Calculated averages for 3 group: Mean normalized or proportional structural parameters in the 3 structural classes. Auton. folding & ind. binding: normalized or proportional structural properties of each protein belonging to ’autonomous folding & independent binding’ Coupled folding & binding: normalized or proportional structural properties of each protein belonging to ’coupled folding & binding’ Mutual synergistic folding: normalized or proportional structural properties of each protein belonging to ’mutual synergistic folding’

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