Journal of Biomolecular NMR

, Volume 67, Issue 4, pp 243–271 | Cite as

Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer



Although Chemical Exchange Saturation Transfer (CEST) type NMR experiments have been used to study chemical exchange processes in molecules since the early 1960s, there has been renewed interest in the past several years in using this approach to study biomolecular conformational dynamics. The methodology is particularly powerful for the study of sparsely populated, transiently formed conformers that are recalcitrant to investigation using traditional biophysical tools, and it is complementary to relaxation dispersion and magnetization transfer experiments that have traditionally been used to study chemical exchange processes. Here we discuss the concepts behind the CEST experiment, focusing on practical aspects as well, we review some of the pulse sequences that have been developed to characterize protein and RNA conformational dynamics, and we discuss a number of examples where the CEST methodology has provided important insights into the role of dynamics in biomolecular function.


CEST Slow conformational exchange Molecular dynamics Excited conformational states 



This work was supported by grants from the Canadian Institutes of Health Research. L.E.K holds a Canada Research Chair in Biochemistry. P.V. is grateful to TIFR Centre for Interdisciplinary Sciences for funding. This paper is dedicated to the memory of Professor Alex Bain, McMaster University, whose pioneering contributions to the NMR chemical exchange field were highly inspirational to the authors.


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Copyright information

© Springer Science+Business Media Dordrecht 2017

Authors and Affiliations

  1. 1.TIFR Centre for Interdisciplinary SciencesHyderabadIndia
  2. 2.Departments of Molecular Genetics, Biochemistry and ChemistryUniversity of TorontoTorontoCanada
  3. 3.Hospital for Sick ChildrenProgram in Molecular Structure and FunctionTorontoCanada

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