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Fig. 5 | Biotechnology for Biofuels

Fig. 5

From: Current and future advances in fluorescence-based visualization of plant cell wall components and cell wall biosynthetic machineries

Fig. 5

Comparison of proteinaceous labeling reagents. a Molecular size of labeling reagents. All figures drawn in PyMol from pdb accession codes 1IGY (IgG), 1BBD (Fab), 4K79 (Lambody), 1MFA (scFv), 1EMA (GFP), 1GUI (CBM4), 1NBC (CBM3), 3P0G (Nanobody), and 5MN2 (Affimer). The IgM structure is a hybrid model (IgM Fv and Cμ1-3 domains from EMD-4945 [135], and Cμ4 and J chain from pdb code 6KXS [136]) in a compact conformation bound to both antigen and complement proteins C1 and C4b (not displayed). Cellulose microfibril modeled with a 34443 habit [137]. b IgG-type domain of a scFv reagent with a trisaccharide antigen binding domain. CDR regions are shown in red sticks and the bound antigen in a white space-filling model. c Nanobody binding in a small cleft of a membrane receptor. CDR regions are shown in red sticks and the receptor in white surface model. d Lambody raised against a disaccharide antigen. Residues in positions with low sequence conservation are drawn in red sticks and the bound antigen in a white space-filling model. Note that this particular structure has 2 LRR-V repeats, but naturally occurring lambodies may have between 1 and 9 repeats. e CBM3a domain with the “planar strip” cellulose binding residues shown in red sticks. f CBM4 domain binding a \(\beta \)-1,3-glucan ligand. Ligand binding residues are highlighted as red sticks around the glucan in a white space-filling model. g Affimer binding to a protein ligand. Randomized residues are highlighted as red sticks with the protein target rendered in a white surface model

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