Related ArticlesEffective rotational correlation times of proteins from NMR relaxation interference.
J Magn Reson. 2006 Jan;178(1):72-6
Authors: Lee D, Hilty C, Wider G, Wüthrich K
Knowledge of the effective rotational correlation times, tauc, for the modulation of anisotropic spin-spin interactions in macromolecules subject to Brownian motion in solution is of key interest for the practice of NMR spectroscopy in structural biology. The value of tauc enables an estimate of the NMR spin relaxation rates, and indicates possible aggregation of the macromolecular species. This paper reports a novel NMR pulse scheme, [15N,1H]-TRACT, which is based on transverse relaxation-optimized spectroscopy and permits to determine tauc for 15N-1H bonds without interference from dipole-dipole coupling of the amide proton with remote protons. [15N,1H]-TRACT is highly efficient since only a series of one-dimensional NMR spectra need to be recorded. Its use is suggested for a quick estimate of the rotational correlation time, to monitor sample quality and to determine optimal parameters for complex multidimensional NMR experiments. Practical applications are illustrated with the 110 kDa 7,8-dihydroneopterin aldolase from Staphylococcus aureus, the uniformly 15N-labeled Escherichia coli outer membrane protein X (OmpX) in 60 kDa mixed OmpX/DHPC micelles with approximately 90 molecules of unlabeled 1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC), and the 16 kDa pheromone-binding protein from Bombyx mori, which cover a wide range of correlation times.
Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins
Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins
Abstract Well-resolved 2Hâ??13C correlation spectra, reminiscent of 1Hâ??13C correlations, are obtained for perdeuterated ubiquitin and for perdeuterated outer-membrane protein G (OmpG) from E. coli by exploiting the favorable lifetime of 2H double-quantum (DQ) states. Sufficient signal-to-noise was achieved due to the short deuterium T 1, allowing for high repetition rates and enabling 3D experiments with a 2Hâ??13C transfer step in a reasonable time....
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ncIDP-assign: A SPARKY extension for the effective NMR assignment of intrinsically disordered proteins.
ncIDP-assign: A SPARKY extension for the effective NMR assignment of intrinsically disordered proteins.
ncIDP-assign: A SPARKY extension for the effective NMR assignment of intrinsically disordered proteins.
Bioinformatics. 2011 Mar 3;
Authors: Tamiola K, Mulder FA
SUMMARY: We describe here the ncIDP-assign extension for the popular NMR assignment programme SPARKY, which aids in the sequence-specific resonance assignment of intrinsically disordered proteins (IDPs). The assignment plugin greatly facilitates the effective matching of a set of...
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[NMR paper] Determination of protein rotational correlation time from NMR relaxation data at vari
Determination of protein rotational correlation time from NMR relaxation data at various solvent viscosities.
Related Articles Determination of protein rotational correlation time from NMR relaxation data at various solvent viscosities.
J Biomol NMR. 2004 Dec;30(4):431-42
Authors: Korchuganov DS, Gagnidze IE, Tkach EN, Schulga AA, Kirpichnikov MP, Arseniev AS
An accurate determination of the overall rotation of a protein plays a crucial role in the investigation of its internal motions by NMR. In the present work, an innovative approach to the...
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[NMR paper] 14N NMR relaxation times of several protein amino acids in aqueous solution--comparis
14N NMR relaxation times of several protein amino acids in aqueous solution--comparison with 17O NMR data and estimation of the relative hydration numbers in the cationic and zwitterionic forms.
Related Articles 14N NMR relaxation times of several protein amino acids in aqueous solution--comparison with 17O NMR data and estimation of the relative hydration numbers in the cationic and zwitterionic forms.
J Magn Reson. 2003 Oct;164(2):294-303
Authors: Troganis AN, Tsanaktsidis C, Gerothanassis IP
The 14N nuclear magnetic resonance (NMR)...
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[NMR paper] A simple and effective NMR cell for studies of encapsulated proteins dissolved in low
A simple and effective NMR cell for studies of encapsulated proteins dissolved in low viscosity solvents.
Related Articles A simple and effective NMR cell for studies of encapsulated proteins dissolved in low viscosity solvents.
J Biomol NMR. 2002 Aug;23(4):311-6
Authors: Flynn PF, Milton MJ, Babu CR, Wand AJ
Application of triple-resonance and isotope-edited-NOE methods to the study of increasingly larger macromolecules and their complexes remains a central goal of solution NMR spectroscopy. The slow reorientational motion of larger molecules...
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[NMR paper] Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurem
Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements.
Eur J Biochem. 1995 Jun 15;230(3):1014-24
Authors: Tjandra N, Kuboniwa H, Ren H, Bax A
The backbone motions of calcium-free Xenopus calmodulin have been characterized by measurements of the 15N...
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08-22-2010 03:41 AM
[NMR paper] Assessing potential bias in the determination of rotational correlation times of prot
Assessing potential bias in the determination of rotational correlation times of proteins by NMR relaxation.
Related Articles Assessing potential bias in the determination of rotational correlation times of proteins by NMR relaxation.
J Biomol NMR. 1999 Feb;13(2):101-12
Authors: Lee AL, Wand AJ
The various factors that influence the reliable and efficient determination of the correlation time describing molecular reorientation of proteins by NMR relaxation methods are examined. Nuclear Overhauser effects, spin-lattice, and spin-spin relaxation...
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Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins
Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins
W. Trent Franks, Kathryn D. Kloepper, Benjamin J. Wylie and Chad M. Rienstra
Journal of Biomolecular NMR; 2007; 39(2); pp 107 - 131
Abstract:
Chemical shift assignment is the first step in all established protocols for structure determination of uniformly labeled proteins by NMR. The explosive growth in recent years of magic-angle spinning (MAS) solid-state NMR (SSNMR) applications is largely attributable to improved methods for backbone and side-chain chemical shift correlation...
Effective rotational correlation times of proteins from NMR relaxation interference.
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