Andreas, Loren B.Stanek, JanLe Marchand, TanguyBertarello, AndreaPaepe, Diane Cala-DeLalli, DanielaKrejcikova, MagdalenaDoyen, CamilleOester, CarlKnott, BennoWegner, SebastianEngelke, FrankFelli, Isabella C.Pierattelli, RobertaDixon, Nicholas E.Emsley, LyndonHerrmann, TorstenPintacuda, Guido2015-09-282015-09-282015-09-28201510.1007/s10858-015-9956-1https://infoscience.epfl.ch/handle/20.500.14299/119002WOS:000357489200003Here we introduce a new pulse sequence for resonance assignment that halves the number of data sets required for sequential linking by directly correlating sequential amide resonances in a single diagonal-free spectrum. The method is demonstrated with both microcrystalline and sedimented deuterated proteins spinning at 60 and 111 kHz, and a fully protonated microcrystalline protein spinning at 111 kHz, with as little as 0.5 mg protein sample. We find that amide signals have a low chance of ambiguous linkage, which is further improved by linking in both forward and backward directions. The spectra obtained are amenable to automated resonance assignment using general-purpose software such as UNIO-MATCH.Magic-angle spinningProtein resonance assignmentProton detectionAutomationtext::journal::journal article::research article