Fig. 5: Fingerprints of A. sydowii proteins and lipids.
From: Structural adaptation of fungal cell wall in hypersaline environment
a Protein region of DP refocused J-INADEQUATE spectra collected using A. sydowii (0.5 M NaCl). b Secondary structure of proteins denoted by 13C chemical shifts of Cα. α-helical and β-strand conformations are in yellow and blue, respectively. The amino acid residues in the mobile fraction (left) and rigid fraction (right) are separated by dash lines. c Box-and-whisker diagrams plotting of the relative water-edited intensities (S/S0) of protein carbon sites in 0 M (purple; n = 11), 0.5 M (green; n = 12) and 2.0 M (blue; n = 10) in three A. sydowii samples with varying salt concentrations. The box contains the 25th to 75th percentiles of dataset. The black center line denotes the median value (50th percentile) and the open box represents the mean. The whiskers mark the 5th and 95th percentiles, with values beyond these upper and lower bounds considered outliers (open circles). All the data points are shown in each concentration. d 2D refocused INEPT 1H-13C correlation spectra of A. sydowii samples cultured with 0 M, 0.5 M, and 2.0 M NaCl. The spectra are compared with the control spectra of model lipids POPC (magenta) and POPG (blue), showing the α, β, and γ carbons in phospholipid headgroups and the carbons in lipid tails. Source data of Fig. 5c are provided as a Source Data file.
