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, 13Cā?² and 1H chemical shift tensors for human ubiquitin and the GB1 and GB3 fragments of staphylococcal protein G. The average and range of variation of the anisotropies is in good agreement with experimental estimates from solid-state NMR, and the variation among residues is somewhat smaller than that estimated from solution-state measurements. Hydrogen-bond effects account for much of the variation, both between helix and sheet regions, and within elements of secondary structure, but other effects (including variations in torsion angles) may play a role as well.
Content Type Journal Article
Category Article
Pages 1-10
DOI 10.1007/s10858-011-9556-7
Authors
Sishi Tang, Department of Chemistry and Chemical Biology, BioMaPS Institute, Rutgers University, Piscataway, NJ 08854, USA
David A. Case, Department of Chemistry and Chemical Biology, BioMaPS Institute, Rutgers University, Piscataway, NJ 08854, USA
Chemical shift prediction for protein structure calculation and quality assessment using an optimally parameterized force field
Chemical shift prediction for protein structure calculation and quality assessment using an optimally parameterized force field
Publication year: 2011
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 23 May 2011</br>
Jakob T., Nielsen , Hamid R., Eghbalnia , Niels Chr., Nielsen</br>
The exquisite sensitivity of chemical shifts as reporters of structural information, and the ability to measure them routinely and accurately, gives great import to formulations that elucidate the structure-chemical-shift relationship. Here we...
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05-24-2011 10:02 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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[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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The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross
The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acs_authorchoice.jpg http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy.
J Am Chem Soc. 2010 Aug 11;132(31):10866-75
...
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08-17-2010 03:36 AM
A device for the measurement of residual chemical shift anisotropy and residual dipol
Abstract Residual dipolar coupling (RDC) and residual chemical shift anisotropy (RCSA) report on orientational properties of a dipolar bond vector and a chemical shift anisotropy principal axis system, respectively. They can be highly complementary in the analysis of backbone structure and dynamics in proteins as RCSAs generally include a report on vectors out of a peptide plane while RDCs usually report on in-plane vectors. Both RDC and RCSA average to zero in isotropic solutions and require partial orientation in a magnetic field to become observable. While the alignment and measurement of...
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08-14-2010 04:19 AM
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...
Calculation of chemical shift anisotropy in proteins
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