Related Experiment Video
Updated: Aug 2, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar
1Protein Engineering Network Centers of Excellence and Department of Medical Genetics, University of Toronto, ON, Canada.
Abstract:
Residual dipolar couplings measured in weakly aligning liquid-crystalline solvent contain valuable information on the structure of biomolecules in solution. Here we demonstrate that dipolar couplings (DCs) can be used to derive a comprehensive set of pairwise angular restraints that do not depend on the orientation of the alignment tensor principal axes. These restraints can be used to assess the agreement between a trial protein structure and a set of experimental dipolar couplings by means of a graphic representation termed a 'DC consistency map'. Importantly, these maps can be used to recognize structural elements consistent with the experimental DC data and to identify structural parameters that require further refinement, which could prove important for the success of DC-based structure calculations. This approach is illustrated for the 42 kDa maltodextrin-binding protein.
Related Concept Videos
Molecular Shapes
Molecular Geometry and Dipole Moments
MO Theory and Covalent Bonding
Newman Projections
The organic molecules rotate across the single bonds leading to numerous temporary three-dimensional structures of varying energy known as conformers.
Fischer Projections
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

