Breaking symmetry in the structure determination of (large) symmetric protein dimers.
J Biomol NMR
; 24(2): 143-8, 2002 Oct.
Article
in En
| MEDLINE
| ID: mdl-12495030
ABSTRACT
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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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Proteins
Language:
En
Journal:
J Biomol NMR
Journal subject:
BIOLOGIA MOLECULAR
/
DIAGNOSTICO POR IMAGEM
/
MEDICINA NUCLEAR
Year:
2002
Type:
Article
Affiliation country:
United States