NMR Studies of Biomolecular Dynamics and Structural Plasticity Using Residual Dipolar Couplings

Due to their exquisite sensitivity to bond vector orientations and distances, residual dipolar couplings are emerging as a powerful NMR methodology for probing the conformational dynamics of biomolecules. The global organization of multi-domain proteins and complexes can now be accurately established in solution, providing insights into distinguishing structural features under different solution environments or with respect to the solid state. Collective motions of domains or secondary structural elements occurring over sub-millisecond timescales, which have resisted characterization using traditional techniques, can now be directly probed using suitable residual dipolar coupling-based techniques. Advances in methods for achieving molecular alignment and data interpretation are enabling characterization of motions with increasingly high resolution. There are now approaches for determining residual dipolar coupling-based generalized order parameters, which can complement their spin relaxation counterparts due to their broader timescale sensitivity. The existence of multiple conformations can now more easily be detected and the residual dipolar coupling data used to confirm or refute models for the conformational fluctuations. It can be expected that future biomolecular NMR studies will increasingly benefit from residual dipolar coupling applications which can recognize and account for molecular flexibility. © 2003 Elsevier Science Ireland Ltd. All rights reserved.

Duke Scholars

Author Hashim Al-Hashimi Biochemistry