Protein dynamics residual dipolar couplings

Fischer MW, Losonczi JA, Weaver JL, Prestegard JH (1999) Domain orientation and dynamics in multidomain proteins from residual dipolar couplings. Biochemistry 38 9013-9022... 

P. Bernado, M. Blackledge, Anisotropic small amplitude peptide plane dynamics in proteins from residual dipolar couplings, J. Am. Chem. Soc. 126 (2004) 4907-4920. 

Conformationally heterogeneous states of proteins can be determined using NMR-derived structural data and suitable molecular dynamics techniques.100 Residual dipolar couplings have been shown to represent motions in ubiquitin slower than its correlation time.101 Using an extensive set of residual dipolar couplings, namely, 36 sets of amide NH, 6 sets of HNC and NC as well as 11... 

Residual dipolar couplings have been used by Mittermaier and Kay187 to probe the torsion angle dynamics of protein side-chains. Using the B1 domain of peptostreptococcal protein L, they show that the residual dipolar couplings can be used to distinguish static from mobile side-chains, and that the motions of most mobile side-chains can be adequately explained by rotamer-jump models. 

The measurement of residual dipolar couplings in weakly aUgned proteins can potentially provide unique information on their structure and dynamics in the solution state. The challenge is to extract the information of interest from the measurements, which normally reflect a convolution of the structural and dynamic properties. Tolman et alP" discussed a formalism which allows a first... 

Meiler et al applied the model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins. Ishima et aO compared the methyl rotation axis order parameters derived from the model-free analyses of the and longitudinal and transverse relaxation rates measured in the same protein sample. Best et al reported the results of molecular dynamics simulations compared with NMR relaxation experiments for maltose and isomaltose. Using the model-free formalism they could estimate reliable order parameters. Baber et used an extended model-... 

Backbone scalar couplings are widely used in NMR studies of structure and dynamics of biomolecules [93]. Additionally, there is a substantial interest in precise determination of residual dipolar couplings for structural studies of weakly oriented biomolecules. Most of the relevant coupling constants in proteins are rather small - of the magnitude from a few to a hundred hertz. Therefore, in order to achieve the sufficient resolution in indirectly measured dimensions, the majority of traditional methods devoted to coupling constants determination in biomolecules are limited to two-dimensional techniques, which frequently suffer from peak overlap. However, the random sampling of evolution time domain allows one to obtain spectra of resolution limited only by transverse relaxation... 

Lakomek NA et al (2008) Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics. J Biomol NMR 41(3) 139-155... 

Meiler J et al (2001) Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins. J Am Chem Soc 123(25) 6098-6107... 

REDCRAFT (Residual Dipolar Coupling Residue v4ssembly and Filtering Tool), a new software tool that uses only experimental data (including RDCs) for structure characterization and identification of dynamics of proteins and polypeptides. 

---