{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["18"],"submitter":["Di Rienzo L"],"pubmed_abstract":["Protein-protein interactions regulate almost all cellular functions and rely on a fine tune of surface amino acids properties involved on both molecular partners. The disruption of a molecular association can be caused even by a single residue mutation, often leading to a pathological modification of a biochemical pathway. Therefore the evaluation of the effects of amino acid substitutions on binding, and the <i>ad hoc</i> design of protein-protein interfaces, is one of the biggest challenges in computational biology. Here, we present a novel strategy for computational mutation and optimization of protein-protein interfaces. Modeling the interaction surface properties using the Zernike polynomials, we describe the shape and electrostatics of binding sites with an ordered set of descriptors"],"journal":["Computational and structural biotechnology journal"],"pagination":["2678-2686"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7548301"],"repository":["biostudies-literature"],"pubmed_title":["A novel strategy for molecular interfaces optimization: The case of Ferritin-Transferrin receptor interaction."],"pmcid":["PMC7548301"],"pubmed_authors":["Di Rienzo L","Testi C","Montemiglio LC","Baiocco P","Milanetti E","Boffi A","Ruocco G"],"additional_accession":[]},"is_claimable":false,"name":"A novel strategy for molecular interfaces optimization: The case of Ferritin-Transferrin receptor interaction.","description":"Protein-protein interactions regulate almost all cellular functions and rely on a fine tune of surface amino acids properties involved on both molecular partners. The disruption of a molecular association can be caused even by a single residue mutation, often leading to a pathological modification of a biochemical pathway. Therefore the evaluation of the effects of amino acid substitutions on binding, and the <i>ad hoc</i> design of protein-protein interfaces, is one of the biggest challenges in computational biology. Here, we present a novel strategy for computational mutation and optimization of protein-protein interfaces. Modeling the interaction surface properties using the Zernike polynomials, we describe the shape and electrostatics of binding sites with an ordered set of descriptors","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020","modification":"2026-05-02T22:55:05.303Z","creation":"2020-10-29T12:39:29Z"},"accession":"S-EPMC7548301","cross_references":{"pubmed":["33101606"],"doi":["10.1016/j.csbj.2020.09.020"]}}