Title

Geometrical and electro-static determinants of protein-protein interactions

Authors

Vicky Kumar², AshitaSood¹, Anjana Munshi³, Tarkeshwar Gautam⁴ & Mahesh Kulharia^1,*

Affiliation

¹Centre for Computational Biology and Bioinformatics, School of Life Sciences, Central University of Himachal Pradesh, Kangra, India, 176206; ²Department of Computational Sciences, School of Basic and Applied Sciences, CentralUniversity of Punjab, Bathinda, India, 151001; ³Department of Human Genetics and Molecular Medicine, School of Health Sciences, Central University of Punjab, Bathinda, India, 151001; ⁴Department of Zoology, Kalindi College, University of Delhi , Delhi, India, 110008; *Corresponding author

Email

Email: kulharia@gmail.com Phone: +91-99884 28856

Article Type

Research Article

Date

Received September 10, 2021; Revised October 12, 2021; Accepted October 12, 2021, Published October 31, 2021

Protein-protein interactions (PPI) are pivotal to the numerous processes in the cell. Therefore, it is of interest to document the analysis of these interactions in terms of binding sites, topology of the interacting structures and physiochemical properties of interacting interfaces and the of forces interactions. The interaction interface of obligatory protein-protein complexes differs from that of the transient interactions. We have created a large database of protein-protein interactions containing over100 thousand interfaces. The structural redundancy was eliminated to obtain a non-redundant database of over 2,265 interaction interfaces. Therefore, it is of interest to document the analysis of these interactions in terms of binding sites, topology of the interacting structures and physiochemical properties of interacting interfaces and the offorces interactions. The residue interaction propensity and all of the rest of the parametric scores converged to a statistical indistinguishable common sub-range and followed the similar distribution trends for all three classes of sequence-based classifications PPInS. This indicates that the principles of molecular recognition are dependent on the preciseness of the fit in the interaction interfaces. Thus, it reinforces the importance of geometrical and electrostatic complementarity as the main determinants for PPIs.

Keywords

Protein-protein interactions; protein-protein interaction interface; non-redundant database; residue interface propensity; hydrophobicity; solvation free energy; planarity; protrusion; depth.

Citation

Kumar et al. Bioinformation 17(10): 851-860 (2021)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.