Transfer residual dipolar couplings

However, if side-chain carbon assignments are wanted, C(CC)(CO)NH experiments [33] that start directly with carbon magnetization and transfer it further to the amide proton for detection are available. If protonated substituents, for example methyl groups, have been introduced into the otherwise perdeuterated protein, the usual HC(C)(CO)NH-TOCSY pulse sequence can be used to obtain the proton chemical shifts. These protons can provide a small number of NOEs that, together with residual dipolar couplings and the secondary structure identification from chemical shifts, make the determination of the global fold of large proteins possible. 

IKK I/cB kinase NBD NEMO binding domain NEMO NF/cB essential modulator NOE Nuclear Overhauser elfect RDC Residual dipolar coupling SAR Structure-activity relationship trCCR Transferred OCR trNOE Transferred NOE... 

R160 S. H. Alarcon and A. C. Olivieri, Residual Dipolar Coupling Effects in Solid State MAS NMR. Investigation of Proton Transfer Processes in Solids p. Pl/263... 

Residual dipolar couplings can be used for coherence transfer in the same manner as the scalar ones. This feature was utilised in the proposed CT-COSY... 

Theoretical analysis of Hartmann-Hahn transfer in the presence of scalar and residual dipolar couplings... 

Side-chain C-C residual dipolar couplings have been measured by Vogeli et in uniformly deuterated and enriched human ubiquitin in the presence of bacteriophages Pfl by the use of the FLOPSY family experiment, one of the many broadband polarization transfer schemes. An excellent correlation between the measured RDCs and the 3D structure of the protein has been observed, indicating a potential use of the C-C RDCs in the structure determination of perdeuterated proteins. 

Kramer and Glaser analysed the transfer efficiency of cross-relaxation compensated (Clean) TOCSY sequences for applications to residual dipolar couplings. Surprisingly most conventional Clean TOCSY sequences are very inefficient for dipolar transfer. It is shown theoretically, that this is a general property of all phase-alternating mixing sequences, i.e., for such sequences the suppression of cross-relaxation excludes dipolar transfer in the spin-diffusion limit. A new family of clean dipolar TOCSY sequences is derived which provides excellent transfer efficiencies for a broad range of offset frequencies. 

The new procedure for determination of the structure of protein-protein complexes using saturation transfer and dipolar couplings has been constructed by Nakamura an co-workers.The SAT and RDC data provide information on the interfacial residues and the relative orientations of the two protein molecules. Docking simulation is then made to reconstruct a complex conformation, which satisfies the experimental data. 

Kramer and Glaser " analysed the transfer efficiency of cross-relaxation compensated (Clean) TOCSY sequenees is analyzed for applications to residual dipolar couplings. Surprisingly most conventional Clean TOCSY sequences are... 

It has been suggested that the relative sign and the magnitude of the scalar and the residual dipolar couplings in homonuclear spin 1/2 systems can be determined based on the sign and the amplitude of the transfer fimctions in a TOCSY experiment. The efficiency of different mixing sequences and different transfer functions has been examined both theoretically and experimentally. The efficiencies of various separated local field (SLF) experiments... 

New Pulse Schemes. A general method for constructing optimized coherence-transfer pulse-sequence elements has been proposed. " As an illustrative application, the method is used to quantitatively measure H- H and H- C residual dipolar eouplings in a 17 kDa protein weakly aligned by means of Pfl phages. The transfer efficiency of cross-relaxation compensated Clean-TOCSY sequences has been analyzed for applications to residual dipolar couplings and it is observed that most conventional sequences are very... 

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