caa a22 4500 445325992 CHVBK 20180317142720.0 cr unu---uuuuu 170323e20110601xx s 000 0 eng 10.1007/s10858-011-9508-2 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9508-2 Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution [Elektronische Daten] [Magnus Kjaergaard, Flemming Poulsen] Random coil chemical shifts are necessary for secondary chemical shift analysis, which is the main NMR method for identification of secondary structure in proteins. One of the largest challenges in the determination of random coil chemical shifts is accounting for the effect of neighboring residues. The contributions from the neighboring residues are typically removed by using neighbor correction factors determined based on each residue's effect on glycine chemical shifts. Due to its unusual conformational freedom, glycine may be particularly unrepresentative for the remaining residue types. In this study, we use random coil peptides containing glutamine instead of glycine to determine the random coil chemical shifts and the neighbor correction factors. The resulting correction factors correlate to changes in the populations of the major wells in the Ramachandran plot, which demonstrates that changes in the conformational ensemble are an important source of neighbor effects in disordered proteins. Glutamine derived random coil chemical shifts and correction factors modestly improve our ability to predict 13C chemical shifts of intrinsically disordered proteins compared to existing datasets, and may thus improve the identification of small populations of transient structure in disordered proteins. Springer Science+Business Media B.V., 2011 Natively unfolded protein nationallicence Peptide nationallicence Secondary chemical shift analysis nationallicence Conformational ensemble nationallicence Transient helix nationallicence Kjaergaard Magnus Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, Copenhagen, Denmark aut Poulsen Flemming Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, Copenhagen, Denmark aut Journal of Biomolecular NMR Springer Netherlands 50/2(2011-06-01), 157-165 0925-2738 50:2<157 2011 50 10858 https://doi.org/10.1007/s10858-011-9508-2 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9508-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kjaergaard Magnus Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, Copenhagen, Denmark aut NATIONALLICENCE 700 1- Poulsen Flemming Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, Copenhagen, Denmark aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 50/2(2011-06-01), 157-165 0925-2738 50:2<157 2011 50 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer