Protein flexibility spans a broad spectrum, from highly stable folded to intrinsically disordered states. In this review, we discuss how various techniques, including X-ray crystallography, nuclear magnetic resonance spectroscopy and ensemble-modeling strategies employing various experimental measurements, have enabled detailed structural and dynamic characterizations of proteins in their free and bound states. This has revealed a variety of possible binding scenarios in which flexibility can either decrease or increase upon binding. Furthermore, dynamic free-state ensembles have repeatedly been observed to contain transiently formed conformations that partially or completely resemble bound states. These results demonstrate an intimate connection between protein flexibility and protein interactions and illustrate the huge diversity of structure and dynamics in both free proteins and protein complexes. © 2012 Elsevier Ltd.
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