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 |
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| Authors: | Ouwen Zhang Lewis E Kay J Paul Olivier Julie D Forman-Kay |
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| Institution: | (1) Biochemistry Research Division, Hospital for Sick Children, 555 University Avenue, M5G 1X8 Toronto, ON, Canada;(2) Protein Engineering Network Centres of Excellence, University of Toronto, M5S 1A8 Toronto, ON, Canada;(3) Department of Medical Genetics, University of Toronto, M5S 1A8 Toronto, ON, Canada;(4) Department of Biochemistry, University of Toronto, M5S 1A8 Toronto, ON, Canada;(5) Department of Chemistry, University of Toronto, M5S 1A8 Toronto, ON, Canada;(6) Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, M5G 1X5 Toronto, ON, Canada |
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| Abstract: | 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.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 |
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| Keywords: | 15N chemical shifts Unfolded state Pulsed field gradients Sensitivity enhanced Water suppression SH3 domain |
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