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15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
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Visualizing side chains of invisible protein conformers by solution NMR

Guillaume Bouvignies1, Pramodh Vallurupalli1, Lewis E Kay2

  • 1Department of Molecular Genetics, The University of Toronto, Toronto, Ontario M5S 1A8, Canada; Department of Biochemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada; Department of Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada.

Journal of Molecular Biology
|November 12, 2013
PubMed
Summary

This study introduces a new NMR method to analyze rare protein structures using side-chain (13)C chemical shifts. This technique provides atomic-level insights into protein folding and dynamics, crucial for understanding biochemical processes.

Keywords:
2DBMRBBiological Magnetic Resonance BankCESTCPMGCarr–Purcell–Meiboom–GillFIDchemical exchange saturation transferchemical shiftsconformationally excited statesfree induction decayprotein side chainstwo-dimensional

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