Journal of Biomolecular NMR

, Volume 4, Issue 5, pp 727–734

A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium

  • Neil A. Farrow
  • Ouwen Zhang
  • Julie D. Forman-Kay
  • Lewis E. Kay
Short Communication

DOI: 10.1007/BF00404280

Cite this article as:
Farrow, N.A., Zhang, O., Forman-Kay, J.D. et al. J Biomol NMR (1994) 4: 727. doi:10.1007/BF00404280

Summary

A heteronuclear correlation experiment is described which permits simultaneous characterization of both 15N longitudinal decay rates and slow conformational exchange rates. Data pertaining to the exchange between folded and unfolded forms of an SH3 domain is used to illustrate the technique. Because the unfolded form of the molecule, on average, shows significantly higher NH exchange rates than the folded form, and approach which minimizes the degree of water saturation is employed, enabling the extraction of accurate rate constants.

Key words

Protein dynamics Chemical exchange Protein folding 

Copyright information

© ESCOM Science Publishers B.V. 1994

Authors and Affiliations

  • Neil A. Farrow
    • 1
    • 2
    • 3
    • 4
  • Ouwen Zhang
    • 1
    • 2
    • 3
    • 4
    • 5
  • Julie D. Forman-Kay
    • 5
  • Lewis E. Kay
    • 1
    • 2
    • 3
    • 4
  1. 1.Protein Engineering Network Centres of ExcellenceUniversity of TorontoTorontoCanada
  2. 2.Department of Molecular and Medical GeneticsUniversity of TorontoTorontoCanada
  3. 3.Department of BiochemistryUniversity of TorontoTorontoCanada
  4. 4.Department of ChemistryUniversity of TorontoTorontoCanada
  5. 5.Division of Biochemistry ResearchHospital for Sick ChildrenTorontoCanada