Journal of Biomolecular NMR

, Volume 4, Issue 6, pp 845–858

Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques

  • Ouwen Zhang
  • Lewis E. Kay
  • J. Paul Olivier
  • Julie D. Forman-Kay
Research Paper

DOI: 10.1007/BF00398413

Cite this article as:
Zhang, O., Kay, L.E., Olivier, J.P. et al. J Biomol NMR (1994) 4: 845. doi:10.1007/BF00398413

Summary

The backbone 1H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter protein, drk, have been assigned. This domain is in slow exchange on the NMR timescale between folded and predominantly unfolded states. Data were collected on both states simultaneously, on samples of the SH3 in near physiological buffer exhibiting an approximately 1:1 ratio of the two states. NMR methods which exploit the chemical shift dispersion of the 15N resonances of unfolded states and pulsed field gradient water suppression approaches for avoiding saturation and dephasing of amide protons which rapidly exchange with solvent were utilized for the assignment.

Keywords

15N chemical shiftsUnfolded statePulsed field gradientsSensitivity enhancedWater suppressionSH3 domain

Abbreviations

2D, 3D

two-, three-dimensional

drkN SH3

N-terminal SH3 domain of Drosophila drk

HSQC

heteronuclear single-quantum spectroscopy

NOE

nuclear Overhauser enhancement

SH3

Src homology domain 3

TOCSY

total correlation spectroscopy

Copyright information

© ESCOM Science Publishers B.V 1994

Authors and Affiliations

  • Ouwen Zhang
    • 1
    • 2
    • 3
    • 4
    • 5
  • Lewis E. Kay
    • 2
    • 3
    • 4
    • 5
  • J. Paul Olivier
    • 6
  • Julie D. Forman-Kay
    • 1
  1. 1.Biochemistry Research DivisionHospital for Sick ChildrenTorontoCanada
  2. 2.Protein Engineering Network Centres of ExcellenceUniversity of TorontoTorontoCanada
  3. 3.Department of Medical GeneticsUniversity of TorontoTorontoCanada
  4. 4.Department of BiochemistryUniversity of TorontoTorontoCanada
  5. 5.Department of ChemistryUniversity of TorontoTorontoCanada
  6. 6.Division of Molecular and Developmental Biology, Samuel Lunenfeld Research InstituteMount Sinai HospitalTorontoCanada