caa a22 4500 445325704 CHVBK 20180317142719.0 cr unu---uuuuu 170323e20110501xx s 000 0 eng 10.1007/s10858-011-9474-8 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9474-8 Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G [Elektronische Daten] [Ling Cai, Daniel Kosov, David Fushman] We performed density functional calculations of backbone 15N shielding tensors in the regions of beta-sheet and turns of protein G. The calculations were carried out for all twenty-four beta-sheet residues and eight beta-turn residues in the protein GB3 and the results were compared with the available experimental data from solid-state and solution NMR measurements. Together with the alpha-helix data, our calculations cover 39 out of the 55 residues (or 71%) in GB3. The applicability of several computational models developed previously (Cai et al. in J Biomol NMR 45:245-253, 2009) to compute 15N shielding tensors of alpha-helical residues is assessed. We show that the proposed quantum chemical computational model is capable of predicting isotropic 15N chemical shifts for an entire protein that are in good correlation with experimental data. However, the individual components of the predicted 15N shielding tensor agree with experiment less well: the computed values show much larger spread than the experimental data, and there is a profound difference in the behavior of the tensor components for alpha-helix/turns and beta-sheet residues. We discuss possible reasons for this. Springer Science+Business Media B.V., 2011 Nitrogen-15 shielding tensor nationallicence Ab initio calculation nationallicence Density-functional calculation nationallicence Beta-sheet nationallicence Turns nationallicence Protein G nationallicence Cai Ling Department of Chemistry and Biochemistry, University of Maryland, 20742, College Park, MD, USA aut Kosov Daniel Department of Chemistry and Biochemistry, University of Maryland, 20742, College Park, MD, USA aut Fushman David Department of Chemistry and Biochemistry, University of Maryland, 20742, College Park, MD, USA aut Journal of Biomolecular NMR Springer Netherlands 50/1(2011-05-01), 19-33 0925-2738 50:1<19 2011 50 10858 https://doi.org/10.1007/s10858-011-9474-8 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9474-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Cai Ling Department of Chemistry and Biochemistry, University of Maryland, 20742, College Park, MD, USA aut NATIONALLICENCE 700 1- Kosov Daniel Department of Chemistry and Biochemistry, University of Maryland, 20742, College Park, MD, USA aut NATIONALLICENCE 700 1- Fushman David Department of Chemistry and Biochemistry, University of Maryland, 20742, College Park, MD, USA aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 50/1(2011-05-01), 19-33 0925-2738 50:1<19 2011 50 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer