Enhancement of bound-state residual dipolar couplings: conformational analysis of lactose bound to Galectin-3.

ABSTRACT: Residual dipolar couplings (RDCs) have proven to be a valuable NMR tool that can provide long-range constraints for molecular structure determination. The constraints are orientational in nature and are, thus, highly complementary to conventional distance constraints from NOE data. This complementarity would seem to extend to the study of the geometry of ligands bound to proteins. However, unlike transferred NOEs, where collection, even with a large excess of free ligand, results in measurements dominated by bound contributions, RDCs of exchanging ligands can be dominated by free-state contributions. Here we present a strategy for enhancement of RDCs from bound states that is based on specifically enhancing the alignment of the protein to which a ligand will bind. The protein is modified b

SUBMITTER: Zhuang T 

PROVIDER: S-EPMC2242564 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature