DiMoVo: a Voronoi tessellation-based method for discriminating crystallographic and biological protein–protein interactions | Zendy

Julie Bernauer | Zendy; Ranjit Prasad Bahadur | Zendy; Françis Rodier | Zendy; Joël Janin | Zendy; Anne Poupon | Zendy

Open Access

DiMoVo: a Voronoi tessellation-based method for discriminating crystallographic and biological protein–protein interactions

Author(s) -

Julie Bernauer,

Ranjit Prasad Bahadur,

Françis Rodier,

Joël Janin,

Anne Poupon

Publication year - 2008

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/btn022

Subject(s) - voronoi diagram , computer science , protein function , protein crystallization , crystal (programming language) , software , task (project management) , monomer , function (biology) , crystallography , chemistry , biological system , computational biology , artificial intelligence , biology , mathematics , biochemistry , geometry , evolutionary biology , engineering , programming language , organic chemistry , systems engineering , crystallization , gene , polymer

Knowledge of the oligomeric state of a protein is often essential for understanding its function and mechanism. Within a protein crystal, each protein monomer is in contact with many others, forming many small interfaces and a few larger ones that are biologically significant if the protein is a homodimer in solution, but not if the protein is monomeric. Telling such 'crystal dimers' from real ones remains a difficult task.

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