期刊
JOURNAL OF BIOMOLECULAR NMR
卷 24, 期 2, 页码 143-148出版社
KLUWER ACADEMIC PUBL
DOI: 10.1023/A:1020948529076
关键词
asymmetry; protein dimer; protein structure; pseudocontact shifts; residual dipolar coupling
We demonstrate a novel methodology to disrupt the symmetry in the NMR spectra of homodimers. A paramagnetic probe is introduced sub-stoichiometrically to create an asymmetric system with the paramagnetic probe residing on only one monomer within the dimer. This creates sufficient magnetic anisotropy for resolution of symmetry-related overlapped resonances and, consequently, detection of pseudocontact shifts and residual dipolar couplings specific to each monomeric component. These pseudocontact shifts can be readily incorporated into existing structure refinement calculations and enable determination of monomer orientation within the dimeric protein. This methodology can be widely used for solution structure determination of symmetric dimers.
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