caa a22 4500 445324953 CHVBK 20180317142717.0 cr unu---uuuuu 170323e20110101xx s 000 0 eng 10.1007/s10858-010-9457-1 doi (NATIONALLICENCE)springer-10.1007/s10858-010-9457-1 Residual dipolar couplings: are multiple independent alignments always possible? [Elektronische Daten] [Victoria Higman, Jonathan Boyd, Lorna Smith, Christina Redfield] RDCs for the 14kDa protein hen egg-white lysozyme (HEWL) have been measured in eight different alignment media. The elongated shape and strongly positively charged surface of HEWL appear to limit the protein to four main alignment orientations. Furthermore, low levels of alignment and the protein's interaction with some alignment media increases the experimental error. Together with heterogeneity across the alignment media arising from constraints on temperature, pH and ionic strength for some alignment media, these data are suitable for structure refinement, but not the extraction of dynamic parameters. For an analysis of protein dynamics the data must be obtained with very low errors in at least three or five independent alignment media (depending on the method used) and so far, such data have only been reported for three small 6-8kDa proteins with identical folds: ubiquitin, GB1 and GB3. Our results suggest that HEWL is likely to be representative of many other medium to large sized proteins commonly studied by solution NMR. Comparisons with over 60 high-resolution crystal structures of HEWL reveal that the highest resolution structures are not necessarily always the best models for the protein structure in solution. The Author(s), 2010 Residual dipolar couplings nationallicence Hen egg-white lysozyme nationallicence Dynamics nationallicence Protein alignment nationallicence Ubiquitin nationallicence Higman Victoria Department of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, UK aut Boyd Jonathan Department of Biochemistry, University of Oxford, South Parks Road, Oxford, UK aut Smith Lorna Department of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, UK aut Redfield Christina Department of Biochemistry, University of Oxford, South Parks Road, Oxford, UK aut Journal of Biomolecular NMR Springer Netherlands 49/1(2011-01-01), 53-60 0925-2738 49:1<53 2011 49 10858 https://doi.org/10.1007/s10858-010-9457-1 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-010-9457-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Higman Victoria Department of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, UK aut NATIONALLICENCE 700 1- Boyd Jonathan Department of Biochemistry, University of Oxford, South Parks Road, Oxford, UK aut NATIONALLICENCE 700 1- Smith Lorna Department of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, UK aut NATIONALLICENCE 700 1- Redfield Christina Department of Biochemistry, University of Oxford, South Parks Road, Oxford, UK aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 49/1(2011-01-01), 53-60 0925-2738 49:1<53 2011 49 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer