Article ID Journal Published Year Pages File Type
5407113 Journal of Magnetic Resonance 2009 5 Pages PDF
Abstract
Heteronuclear dipole-to-dipole cross-relaxation has been applied to exploring intermolecular interactions and intramolecular spatial proximities in a large supramolecular structure comprised of a β-barrel membrane protein, OmpX, in complex with a polymeric surfactant, amphipol A8-35. The experiments, performed in either the laboratory or the rotating frame, reveal the existence of intermolecular contacts between aromatic amino acids and specific groups of the polymer, in addition to intra-protein dipolar interactions, some of them involving carbonyl carbons. This study opens the perspective of collecting by NMR spectroscopy a new kind of through-space structural information involving aromatic and carbonyl 13C atoms of large proteins.
Related Topics
Physical Sciences and Engineering Chemistry Physical and Theoretical Chemistry
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