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CoMoDo: Identifying Dynamic Protein Domains Based on Covariances of Motion

2015; American Chemical Society; Volume: 11; Issue: 6 Linguagem: Inglês

10.1021/acs.jctc.5b00150

1549-9626

Silke A. Wieninger, G. Matthias Ullmann,

Microbial Metabolic Engineering and Bioproduction

Most large proteins are built of several domains, compact units which enable functional protein motions. Different domain assignment approaches exist, which mostly rely on concepts of stability, folding, and evolution. We describe the automatic assignment method CoMoDo, which identifies domains based on protein dynamics. Covariances of atomic fluctuations, here calculated by an Elastic Network Model, are used to group residues into domains of different hierarchical levels. The so-called dynamic domains facilitate the study of functional protein motions involved in biological processes like ligand binding and signal transduction. By applying CoMoDo to a large number of proteins, we demonstrate that dynamic domains exhibit features absent in the commonly assigned structural domains, which can deliver insight into the interactions between domains and between subunits of multimeric proteins. CoMoDo is distributed as free open source software at www.bisb.uni-bayreuth.de/CoMoDo.html .