[NMR paper] Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS.

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Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS.

Related Articles Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS.

J Biomol NMR. 2013 Jun 29;

Authors: Barbet-Massin E, Pell AJ, Jaudzems K, Franks WT, Retel JS, Kotelovica S, Akopjana I, Tars K, Emsley L, Oschkinat H, Lesage A, Pintacuda G

Abstract
We present here (1)H-detected triple-resonance H/N/C experiments that incorporate CO-CA and CA-CB out-and-back scalar-transfer blocks optimized for robust resonance assignment in biosolids under ultra-fast magic-angle spinning (MAS). The first experiment, (H)(CO)CA(CO)NH, yields (1)H-detected inter-residue correlations, in which we record the chemical shifts of the CA spins in the first indirect dimension while during the scalar-transfer delays the coherences are present only on the longer-lived CO spins. The second experiment, (H)(CA)CB(CA)NH, correlates the side-chain CB chemical shifts with the NH of the same residue. These high sensitivity experiments are demonstrated on both fully-protonated and 100*%-H(N) back-protonated perdeuterated microcrystalline samples of Acinetobacter phage 205 (AP205) capsids at 60*kHz MAS.


PMID: 23812971 [PubMed - as supplied by publisher]



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