Related ArticlesTROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution.
Trends Biochem Sci. 2000 Oct;25(10):462-8
Authors: Riek R, Pervushin K, Wüthrich K
TROSY and CRINEPT are new techniques for solution NMR studies of molecular and supramolecular structures. They allow the collection of high-resolution spectra of structures with molecular weights >100 kDa, significantly extending the range of macromolecular systems that can be studied by NMR in solution. TROSY has already been used to map protein-protein interfaces, to conduct structural studies on membrane proteins and to study nucleic acid conformations in multimolecular assemblies. These techniques will help us to investigate the conformational states of individual macromolecular components and will support de novo protein structure determination in large supramolecular structures.
Combining NMR ensembles and molecular dynamics simulations provides more realistic models of protein structures in solution and leads to better chemical shift prediction
Combining NMR ensembles and molecular dynamics simulations provides more realistic models of protein structures in solution and leads to better chemical shift prediction
Abstract While chemical shifts are invaluable for obtaining structural information from proteins, they also offer one of the rare ways to obtain information about protein dynamics. A necessary tool in transforming chemical shifts into structural and dynamic information is chemical shift prediction. In our previous work we developed a method for 4D prediction of protein 1H chemical shifts in which molecular motions, the...
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02-11-2012 10:31 AM
TROSY NMR Spectroscopy of Large Soluble Proteins.
TROSY NMR Spectroscopy of Large Soluble Proteins.
TROSY NMR Spectroscopy of Large Soluble Proteins.
Top Curr Chem. 2011 Sep 17;
Authors: Xu Y, Matthews S
Abstract
Solution nuclear magnetic resonance spectroscopy is usually only used to study proteins with molecular weight not exceeding about 50 kDa. This size limit has been lifted significantly in recent years, thanks to the development of labelling methods and the application of transverse-relaxation optimized spectroscopy (TROSY). In particular, methyl-specific labelling and...
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09-20-2011 03:10 PM
Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view.
Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view.
Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view.
J Magn Reson. 2011 Mar 30;
Authors: Kay LE
With the development of appropriate labeling schemes and the associated experiments that exploit them it has become possible to record high quality solution NMR spectra of supra-molecular complexes with molecular masses extending to 1MDa. One such approach involves selective (13)CH(3) methyl labeling in highly deuterated proteins...
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04-05-2011 10:22 PM
Solution NMR Spectroscopy of Supra-Molecular Systems, Why Bother? A Methyl TROSY View
Solution NMR Spectroscopy of Supra-Molecular Systems, Why Bother? A Methyl TROSY View
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 8 March 2011</br>
Lewis E., Kay</br>
With the development of appropriate labeling schemes and the associated experiments that exploit them it has become possible to record high quality solution NMR spectra of supra-molecular complexes with molecular masses extending to 1MDa. One such approach involves selective 13CH3 methyl labeling in highly deuterated proteins using experiments that make...
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03-09-2011 04:23 PM
Very simple combination of TROSY, CRINEPT and multiple quantum coherence for signal enhancement in an HN(CO)CA experiment for large proteins
Very simple combination of TROSY, CRINEPT and multiple quantum coherence for signal enhancement in an HN(CO)CA experiment for large proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 3 February 2011</br>
Monika, Bayrhuber , Roland, Riek</br>
Sensitivity enhancement in liquid state nuclear magnetic resonance (NMR) triple resonance experiments for the sequential assignment of proteins is important for the investigation of large proteins or protein complexes. We present here the 3D TROSY-MQ/CRINEPT-HN(CO)CA which makes...
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02-04-2011 07:03 AM
TROSY-selected ZZ-exchange experiment for characterizing slow chemical exchange in large proteins
TROSY-selected ZZ-exchange experiment for characterizing slow chemical exchange in large proteins
Abstract A TROSY-selected ZZ-exchange experiment is described for measuring slow chemical exchange rates by monitoring the TROSY component of 15N longitudinal magnetization. Application of the proposed pulse sequence to the cadherin 8 N-terminal extracelluar domain demonstrates that enhanced sensitivity is obtained, compared to a previously described TROSY-detected ZZ-exchange sequence (Sahu et al. J Am Chem Soc 129: 13232â??13237, 2007), by preserving the TROSY effect during the mixing...
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01-09-2011 12:46 PM
[NMR paper] Determining the structures of large proteins and protein complexes by NMR.
Determining the structures of large proteins and protein complexes by NMR.
Related Articles Determining the structures of large proteins and protein complexes by NMR.
Trends Biotechnol. 1998 Jan;16(1):22-34
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional NMR methodology to obtain 1H, 15N and 13C resonance assignments, interproton-distance and torsion-angle restraints, and restraints that characterize long-range order have, coupled with new methods of structure refinement, permitted solution structure of proteins in excess...
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11-17-2010 11:06 PM
[Louic Vermeer blog] Using procheck_nmr on a large number of structures
Using procheck_nmr on a large number of structures
After a structure calculation with the aria 2.2 software I used aqua and procheck_nmr to assess the result. Although procheck_nmr worked fine on my 20 refined structures (in aria’s refine directory), it ran into trouble with the 100 structures after iteration 8 (directory it8): * Restraints read in from file: * allpdb.nrv
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TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution
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