Backbone importance for protein-protein binding

• Type: Article in International Scientific Journal
• Date: 2007

Authors

Irina S Moreira (Author) Other; Pedro A Fernandes (Author) FCUP; Maria J Ramos (Author) FCUP

Journal

Title: Journal of Chemical Theory and Computation

Vol. 3

Pages: 885-893

ISSN: 1549-9618

Publisher: American Chemical Society

Indexing

ISI Web of Knowledge - 13 Citations

Scopus - 12 Citations

Scientific classification

FOS: Natural sciences > Chemical sciences

Other information

Authenticus ID: P-004-ABG

DOI: 10.1021/ct6003824

Abstract (EN): Although a number of studies have focused on the physical and chemical properties of protein-protein interfaces of complexes to determine their unique features, the importance of the backbone hydrogen bonds to protein-protein binding has been neglected due to the difficulty of quantitatively measuring their contribution to the free binding energy. In this study we are presenting a computational approach that allows the estimation of the contribution to the free binding energy of the CO and NH groups of the backbone of various proteic complexes. A correlation between the quantitative calculated free binding energy contribution of the CO and NH backbone groups of the interfacial residues and the qualitative values expected for this kind of interaction was achieved. The contribution of the backbone to the Delta Delta G(binding) is significant. The average Delta Delta G(binding) contribution of the intermolecular hydrogen bonds of the backbone is 1.77 kcal/mol, which is very similar to the average contribution of the different side chains to the Delta Delta G(binding), with a value of 1.75 kcal/mol. Therefore, the application of this computational approach as well as an alanine scanning mutagenesis study is essential to a more detailed comprehensive knowledge of proteic complex formation.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 9