[NMR paper] Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information.
Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information.
Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information.
J Biomol NMR. 2013 Apr 28;
Authors: Fritzsching KJ, Yang Y, Schmidt-Rohr K, Hong M
Abstract
We introduce a Python-based program that utilizes the large database of (13)C and (15)N chemical shifts in the Biological Magnetic...
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04-30-2013 10:21 PM
Calculation of chemical shift anisotropy in proteins
Calculation of chemical shift anisotropy in proteins
Abstract Individual peptide groups in proteins must exhibit some variation in the chemical shift anisotropy (CSA) of their constituent atoms, but not much is known about the extent or origins of this dispersion. Direct spectroscopic measurement of CSA remains technically challenging, and theoretical methods can help to overcome these limitations by estimating shielding tensors for arbitrary structures. Here we use an automated fragmentation quantum mechanics/molecular mechanics (AF-QM/MM) approach to compute 15N, 13Câ?² and 1H...
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08-29-2011 06:41 AM
SHIFTX2: significantly improved protein chemical shift prediction
SHIFTX2: significantly improved protein chemical shift prediction
Abstract A new computer program, called SHIFTX2, is described which is capable of rapidly and accurately calculating diamagnetic 1H, 13C and 15N chemical shifts from protein coordinate data. Compared to its predecessor (SHIFTX) and to other existing protein chemical shift prediction programs, SHIFTX2 is substantially more accurate (up to 26% better by correlation coefficient with an RMS error that is up to 3.3Ã? smaller) than the next best performing program. It also provides significantly more coverage (up to 10% more),...
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04-01-2011 09:31 PM
[NMR paper] Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
Related Articles Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
J Am Chem Soc. 2005 Aug 31;127(34):11946-7
Authors: Wylie BJ, Franks WT, Graesser DT, Rienstra CM
In this Communication, we introduce a 3D magic-angle spinning recoupling experiment that correlates chemical shift...
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12-01-2010 06:56 PM
[NMR paper] Determination of chemical shift anisotropy tensors of carbonyl nuclei in proteins thr
Determination of chemical shift anisotropy tensors of carbonyl nuclei in proteins through cross-correlated relaxation in NMR.
Related Articles Determination of chemical shift anisotropy tensors of carbonyl nuclei in proteins through cross-correlated relaxation in NMR.
Chemphyschem. 2004 Jun 21;5(6):807-14
Authors: Cisnetti F, Loth K, Pelupessy P, Bodenhausen G
The principal components and orientations of the chemical shift anisotropy (CSA) tensors of nearly all 13C carbonyl nuclei in a small protein have been determined in isotropic solution...
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11-24-2010 09:51 PM
[NMR paper] Heteronuclear NMR studies of cobalt corrinoids. 20. 31P chemical shift anisotropy of
Heteronuclear NMR studies of cobalt corrinoids. 20. 31P chemical shift anisotropy of aquacobalamin and its complex with a haptocorrin from chicken serum.
Related Articles Heteronuclear NMR studies of cobalt corrinoids. 20. 31P chemical shift anisotropy of aquacobalamin and its complex with a haptocorrin from chicken serum.
J Inorg Biochem. 1998 Sep;71(3-4):199-204
Authors: Brown KL, Wilson WW, Jacobsen DW
Static light scattering measurements have been used to determine the molecular mass (65.3 kDa) and second virial coefficient (3.66 x 10(-4)...
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11-17-2010 11:15 PM
Determination of relative tensor orientations by ?-encoded chemical shift anisotropy/
Determination of relative tensor orientations by ?-encoded chemical shift anisotropy/heteronuclear dipolar coupling 3D NMR spectroscopy in biological solids.
Related Articles Determination of relative tensor orientations by ?-encoded chemical shift anisotropy/heteronuclear dipolar coupling 3D NMR spectroscopy in biological solids.
Phys Chem Chem Phys. 2010 Oct 8;
Authors: Hou G, Paramasivam S, Byeon IJ, Gronenborn AM, Polenova T
In this paper, we present 3D chemical shift anisotropy (CSA)/dipolar coupling correlation experiments, based on ?-encoded...
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10-12-2010 02:52 PM
chemical shift anisotropy (CSA) in model-free approach
Hi !
I have a quite general question about the value used for the CSA while studying protein dynamics of 15N-1H vectors with model-free approach.
In the litterature, we mainly find two values for the CSA (-160 and -172 ppm).
There is, if I understand well, a link between the bond length and the CSA, but everyone seems to agree about using the same value of 1.02 A which should give rise to a mean S2 of 0.85 for secondary structure when combined to a CSA of -172 ppm. When using a CSA of -160 ppm, the mean S2 for secondary structure should slightly rise up from 0.85.
The manuals for...
Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints
Linear Mode
