Statistical properties of protein-protein interfaces

DOI10.3390/A8020092MaRDI QIDQ1736641zbMATH OpenOpenAlexFDO

Authors Mihaly Mezei

Publication date 26 March 2019

Published in Algorithms (Search for Journal in Brave)

Copyright license Creative Commons Attribution 4.0 International

Full work available at URL https://doi.org/10.3390/a8020092

zbMATH Keywords

accessible surfacecircular variancemutual proximityresidue propensity

Mathematics Subject Classification ID

Applications of statistics to biology and medical sciences; meta analysis (62P10) Protein sequences, DNA sequences (92D20)

Review text

Summary: The properties of 1172 protein complexes (downloaded from the Protein Data Bank (PDB)) have been studied based on the concept of circular variance as a buriedness indicator and the concept of mutual proximity as a parameter-free definition of contact. The propensities of residues to be in the protein, on the surface or form contact, as well as residue pairs to form contact were calculated. In addition, the concept of circular variance has been used to compare the ruggedness and shape of the contact surface with the overall surface.

Recommendations

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Cited in

(4)

• A statistical measure of association and a series expansion of chain conformations
• Non-covalent interactions across subunit interfaces in Sm proteins
• Interface surfaces for protein-protein complexes
• Use of circular variance to quantify the deviation of a macromolecule from the spherical shape

Describes a project that uses

Uses Software

• COCOMAPS
• SCOWLP
• ProtorP

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