caa a22 4500 445325895 CHVBK 20180317142720.0 cr unu---uuuuu 170323e20110801xx s 000 0 eng 10.1007/s10858-011-9524-2 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9524-2 Structure-based prediction of methyl chemical shifts in proteins [Elektronische Daten] [Aleksandr Sahakyan, Wim Vranken, Andrea Cavalli, Michele Vendruscolo] Protein methyl groups have recently been the subject of much attention in NMR spectroscopy because of the opportunities that they provide to obtain information about the structure and dynamics of proteins and protein complexes. With the advent of selective labeling schemes, methyl groups are particularly interesting in the context of chemical shift based protein structure determination, an approach that to date has exploited primarily the mapping between protein structures and backbone chemical shifts. In order to extend the scope of chemical shifts for structure determination, we present here the CH3Shift method of performing structure-based predictions of methyl chemical shifts. The terms considered in the predictions take account of ring current, magnetic anisotropy, electric field, rotameric type, and dihedral angle effects, which are considered in conjunction with polynomial functions of interatomic distances. We show that the CH3Shift method achieves an accuracy in the predictions that ranges from 0.133 to 0.198ppm for 1H chemical shifts for Ala, Thr, Val, Leu and Ile methyl groups. We illustrate the use of the method by assessing the accuracy of side-chain structures in structural ensembles representing the dynamics of proteins. Springer Science+Business Media B.V., 2011 Protein side-chains nationallicence Methyl groups nationallicence Chemical shift prediction nationallicence Random coil nationallicence Sahakyan Aleksandr Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW, Cambridge, UK aut Vranken Wim European Bioinformatics Institute, Wellcome Trust Genome Campus, CB10 1SD, Cambridge, UK aut Cavalli Andrea Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW, Cambridge, UK aut Vendruscolo Michele Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW, Cambridge, UK aut Journal of Biomolecular NMR Springer Netherlands 50/4(2011-08-01), 331-346 0925-2738 50:4<331 2011 50 10858 https://doi.org/10.1007/s10858-011-9524-2 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9524-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Sahakyan Aleksandr Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW, Cambridge, UK aut NATIONALLICENCE 700 1- Vranken Wim European Bioinformatics Institute, Wellcome Trust Genome Campus, CB10 1SD, Cambridge, UK aut NATIONALLICENCE 700 1- Cavalli Andrea Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW, Cambridge, UK aut NATIONALLICENCE 700 1- Vendruscolo Michele Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW, Cambridge, UK aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 50/4(2011-08-01), 331-346 0925-2738 50:4<331 2011 50 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer