Fig. 3: Detailed rate comparison between different systems.
From: Emergence of a short peptide based reductase via activation of the model hydride rich cofactor
a Bar diagram of the product (2) yield in the presence of different systems at 12 h, b TEM micrograph of BET-16, inset: zoomed portion shows the hollow interior of BET-16 nanotubes indicated by red arrows, c AFM image of BET-16 with line profile (used for showing the height of the bilayer in the dotted box). d CD and FTIR (deconvoluted at amide I region, between 1600 and 1700 cm−1) profile (inset) of BET-16 assemblies, e TEM micrograph of GNPneg bound BET-16 nanotubes, f CLSM micrograph of Coumarin 343 bound BET-16. All the microscopic experiments were repeated for at least three times. g Zeta potential of BET-16 in presence of variable NaBH4 concentration, h normalized 11B NMR profile of NaBH4 in presence and absence of BET-16. The error bars are calculated from three separate experiments. Data are presented as the mean ± s.d. (n = 3 independent experiments). For the bar diagram, statistics for all control systems were estimated using two-sided homoscedastic ‘t’ tests in comparison with the BET-16 system taken as reference (*p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001; exact p value for ARG-16 system is 0.0082, GLU-16 is 0.0008, LYS-16 is 0.0012, HIS-16 is 0.0009, BET-16-HFIP is 0.0010, BET-16-Na2SO4 is 0.0012, BET-16 without NaBH4 is 0.0006 and BET-16-NADH system is 0.0006). Source data are provided as a Source Data file.
