caa a22 4500 445325178 CHVBK 20180317142718.0 cr unu---uuuuu 170323e20111101xx s 000 0 eng 10.1007/s10858-011-9556-7 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9556-7 Calculation of chemical shift anisotropy in proteins [Elektronische Daten] [Sishi Tang, David Case] 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, 13C′ 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. Springer Science+Business Media B.V., 2011 Chemical shift nationallicence Anisotropy nationallicence Proteins nationallicence Tang Sishi Department of Chemistry and Chemical Biology, BioMaPS Institute, Rutgers University, 08854, Piscataway, NJ, USA aut Case David Department of Chemistry and Chemical Biology, BioMaPS Institute, Rutgers University, 08854, Piscataway, NJ, USA aut Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 303-312 0925-2738 51:3<303 2011 51 10858 https://doi.org/10.1007/s10858-011-9556-7 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9556-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Tang Sishi Department of Chemistry and Chemical Biology, BioMaPS Institute, Rutgers University, 08854, Piscataway, NJ, USA aut NATIONALLICENCE 700 1- Case David Department of Chemistry and Chemical Biology, BioMaPS Institute, Rutgers University, 08854, Piscataway, NJ, USA aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 303-312 0925-2738 51:3<303 2011 51 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer