MUSIC and Aromatic Residues: Amino Acid Type-Selective 1H–15N Correlations, III

Human Protein N-terminal Acetyltransferase hNaa50p (hNAT5/hSAN) Follows Ordered Sequential Catalytic Mechanism

“…The spectra were processed with NMRPipe (31) and analyzed using Cara (32). For further diminishing of side chain ambiguity, three-dimensional CC(CO)NH (33,34) and several two-dimensional 1 H-15 N MUSIC (multiplicity selective in-phase coherence transfer) (35)(36)(37) experiments were conducted on the Bruker BioSpin AV600 spectrometer. The 1 H and 13 C chemical shifts were referenced to 4,4-dimethyl-4-silapentane-1-sulfonic acid as an internal standard.…”

The solution structure of an N‐terminally truncated version of the yeast CDC24p PB1 domain shows a different β‐sheet topology

“…NMR data were processed using the XWINNMR software (Bruker), except the 4D spectra, which were processed with NMRPipe [20]. 3D CBCA-(CO)NH/CBCANH, HA(CO)NH/HANH and HNCO/HN(CA)CO experiment pairs [21] and a set of sidechain-selective 2D 1 H-15 N heteronuclear single quantum coherence (HSQC) experiments [22][23][24][25] were recorded as a basis for backbone resonance assignments. Assignments were obtained by employing SAMPA (results to be published), and completed manually using SPARKY [26].…”

BEST-HNN and 2D-(HN)NH experiments for rapid backbone assignment in proteins

“…Several methods have also been introduced earlier for identifying amino acid types in the NMR spectra [17][18][19][20][21][22][23][24]. These include side chain based methods [17][18][19][20], 2D-(HC)NH [25], MUSIC sequences [23,24], HADA-MAC method [22] and the method proposed by Barnwal et al [21] which is based on using combination of chemical shifts [21]. However, the main advantage of the method proposed here lies in the fact that 2D-(HN)NH experiment is applicable to deuterated proteins as well.…”