caa a22 4500 445325216 CHVBK 20180317142718.0 cr unu---uuuuu 170323e20111101xx s 000 0 eng 10.1007/s10858-011-9531-3 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9531-3 Linser Rasmus Analytical Centre and School of Chemistry, University of New South Wales, 2052, Sydney, NSW, Australia aut Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers [Elektronische Daten] [Rasmus Linser] Proteins with excessive deuteration give access to proton detected solid-state NMR spectra of extraordinary resolution and sensitivity. The high spectral quality achieved after partial proton back-exchange has been shown to start a new era for backbone assignment, protein structure elucidation, characterization of protein dynamics, and access to protein parts undergoing motion. The large absence of protons at non-exchangeable sites, however, poses a serious hurdle for characterization of side chains, which play an important role especially for structural understanding of the protein core and the investigation of protein-protein and protein-ligand interactions, e.g. This has caused the perdeuteration approach to almost exclusively be amenable to backbone characterization only. In this work it is shown that a combination of isotropic 13C mixing with long-range 1H/13C magnetization transfers can be used effectively to also access complete sets of side-chain chemical shifts in perdeuterated proteins and correlate these with the protein backbone with high unambiguity and resolution. COmbined POlarization from long-Range transfers And Direct Excitation (COPORADE) allows this strategy to yield complete sets of aliphatic amino acid resonances with reasonable sensitivity. Springer Science+Business Media B.V., 2011 MAS solid-state NMR nationallicence Magic Angle Spinning nationallicence Perdeuteration nationallicence Proton detection nationallicence TOBSY nationallicence Side-chain assignment nationallicence Micro-crystalline proteins nationallicence Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 221-226 0925-2738 51:3<221 2011 51 10858 https://doi.org/10.1007/s10858-011-9531-3 text/html Onlinezugriff via DOI 1 brief-communication jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9531-3 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Linser Rasmus Analytical Centre and School of Chemistry, University of New South Wales, 2052, Sydney, NSW, Australia aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 221-226 0925-2738 51:3<221 2011 51 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer