Probing the diverse landscape of protein flexibility and binding

Joseph A Marsh, Sarah A Teichmann, Julie D Forman-Kay

Research output: Contribution to journalArticlepeer-review


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.
Original languageEnglish
Pages (from-to)643-50
Number of pages8
JournalCurrent opinion in structural biology
Issue number5
Publication statusPublished - Oct 2012


  • Chemistry Techniques, Analytical
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Proteins

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