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...
Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH
Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH
Abstract Secondary chemical shift analysis is the main NMR method for detection of transiently formed secondary structure in intrinsically disordered proteins. The quality of the secondary chemical shifts is dependent on an appropriate choice of random coil chemical shifts. We report random coil chemical shifts and sequence correction factors determined for a GGXGG peptide series following the approach of Schwarzinger et al. (J Am Chem Soc 123(13):2970â??2978, 2001). The chemical shifts are...
[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
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 Tensor – the Heart of NMR : Insights into Biological Aspects of Protei
Chemical Shift Tensor – the Heart of NMR : Insights into Biological Aspects of Proteins
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 7 May 2010</br>
Hazime, Saitô , Isao, Ando , Ayyalusamy, Ramamoorthy</br>
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08-16-2010 03:50 AM
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...