title: Predicting Allosteric Changes from Conformational Ensembles.
abstract: In this issue of Structure, Greener et al. (2017) describe a new computational approach to generate conformational ensembles of proteins based on two experimental input structures. The method shows promise for rapidly predicting global protein flexibility and for the identification of putative binding sites for allosteric effectors on proteins.
authors.affiliation: Physics Department T38, Technical University of Munich, James-Franck-Straße 1, 85748 Garching, Germany; Center for Integrated Protein Science, 81377 Munich, Germany. Electronic address: martin.zacharias@mytum.de.
authors.forename: Martin
authors.initials: M
authors.lastname: Zacharias
mesh_terms: D000494:Allosteric Regulation; D001665:Binding Sites; D019295:Computational Biology / Q000379:methods*; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins