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Curr Opin Struct Biol. 2015 Dec;35:17-23. doi: 10.1016/j.sbi.2015.07.007. Epub 2015 Aug 6.

Adaptability of protein structures to enable functional interactions and evolutionary implications.

Author information

1
Department of Chemical Engineering and Polymer Research Center, and Center for Life Sciences and Technologies, Bogazici University, 34342 Istanbul, Turkey; Department of Computational and Systems Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15260, USA.
2
Department of Computational and Systems Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15260, USA. Electronic address: bahar@pitt.edu.

Abstract

Several studies in recent years have drawn attention to the ability of proteins to adapt to intermolecular interactions by conformational changes along structure-encoded collective modes of motions. These so-called soft modes, primarily driven by entropic effects, facilitate, if not enable, functional interactions. They represent excursions on the conformational space along principal low-ascent directions/paths away from the original free energy minimum, and they are accessible to the protein even before protein-protein/ligand interactions. An emerging concept from these studies is the evolution of structures or modular domains to favor such modes of motion that will be recruited or integrated for enabling functional interactions. Structural dynamics, including the allosteric switches in conformation that are often stabilized upon formation of complexes and multimeric assemblies, emerge as key properties that are evolutionarily maintained to accomplish biological activities, consistent with the paradigm sequence→structure→dynamics→function where 'dynamics' bridges structure and function.

PMID:
26254902
PMCID:
PMC4688206
DOI:
10.1016/j.sbi.2015.07.007
[Indexed for MEDLINE]
Free PMC Article

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