Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 45, Issue 4, Pages 343-349Publisher
SPRINGER
DOI: 10.1007/s10858-009-9382-3
Keywords
J-coupling; Conformation; IDP; IUP; HNHA
Categories
Funding
- European Molecular Biology Organization (EMBO)
- VIDI
- Netherlands Organization for Scientific Research (NWO)
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An experiment is presented to determine (3)J(HNH alpha) coupling constants, with significant advantages for applications to unfolded proteins. The determination of coupling constants for the peptide chain using 1D H-1, or 2D and 3D H-1-N-15 correlation spectroscopy is often hampered by extensive resonance overlap when dealing with flexible, disordered proteins. In the experiment detailed here, the overlap problem is largely circumvented by recording H-1-C-13' correlation spectra, which demonstrate superior resolution for unfolded proteins. J-coupling constants are extracted from the peak intensities in a pair of 2D spin-echo difference experiments, affording rapid acquisition of the coupling data. In an application to the cytoplasmic domain of human neuroligin-3 (hNlg3cyt) data were obtained for 78 residues, compared to 54 coupling constants obtained from a 3D HNHA experiment. The coupling constants suggest that hNlg3cyt is intrinsically disordered, with little propensity for structure.
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