Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 28, Issue 3, Pages 205-212Publisher
SPRINGER
DOI: 10.1023/B:JNMR.0000013706.09264.36
Keywords
deuteration; ILV-labeling; NMR structural accuracy; pseudocontact shifts; residual dipolar coupling; STAT4
Categories
Ask authors/readers for more resources
We demonstrate improved accuracy in protein structure determination for large (greater than or equal to 30 kDa), deuterated proteins (e.g. STAT4(NT)) via the combination of pseudocontact shifts for amide and methyl protons with the available NOEs in methyl-protonated proteins. The improved accuracy is cross validated by Q-factors determined from residual dipolar couplings measured as a result of magnetic susceptibility alignment. The paramagnet is introduced via binding to thiol-reactive EDTA, and multiple sites can be serially engineered to obtain data from alternative orientations of the paramagnetic anisotropic susceptibility tensor. The technique is advantageous for systems where the target protein has strong interactions with known alignment media.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available