caa a22 4500 445325100 CHVBK 20180317142717.0 cr unu---uuuuu 170323e20110201xx s 000 0 eng 10.1007/s10858-011-9472-x doi (NATIONALLICENCE)springer-10.1007/s10858-011-9472-x Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH [Elektronische Daten] [Magnus Kjaergaard, Søren Brander, Flemming Poulsen] 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):2970-2978, 2001). The chemical shifts are determined at neutral pH in order to match the conditions of most studies of intrinsically disordered proteins. Temperature has a non-negligible effect on the 13C random coil chemical shifts, so temperature coefficients are reported for the random coil chemical shifts to allow extrapolation to other temperatures. The pH dependence of the histidine random coil chemical shifts is investigated in a titration series, which allows the accurate random coil chemical shifts to be obtained at any pH. By correcting the random coil chemical shifts for the effects of temperature and pH, systematic biases of the secondary chemical shifts are minimized, which will improve the reliability of detection of transient secondary structure in disordered proteins. Springer Science+Business Media B.V., 2011 Natively unfolded protein nationallicence Peptide nationallicence NMR nationallicence Protonation state nationallicence Secondary chemical shift analysis nationallicence Kjaergaard Magnus Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, København N, Denmark aut Brander Søren Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, København N, Denmark aut Poulsen Flemming Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, København N, Denmark aut Journal of Biomolecular NMR Springer Netherlands 49/2(2011-02-01), 139-149 0925-2738 49:2<139 2011 49 10858 https://doi.org/10.1007/s10858-011-9472-x text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9472-x text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kjaergaard Magnus Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, København N, Denmark aut NATIONALLICENCE 700 1- Brander Søren Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, København N, Denmark aut NATIONALLICENCE 700 1- Poulsen Flemming Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, København N, Denmark aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 49/2(2011-02-01), 139-149 0925-2738 49:2<139 2011 49 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer