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. 2016 Mar 29;110(6):1280–1290. doi: 10.1016/j.bpj.2015.12.042

Figure 1.

Figure 1

T4 Lysozyme as a model system and single-molecule folding experimental setup. (a) Cartoon representation of T4 Lysozyme (PDB: 2LZM). Highlighted is the N-terminal A-helix (beige, residues 1–11), the N-terminal subdomain (red, residues 12–66), and the C-terminal subdomain (cyan, resides 67–164). Also shown are the attachment points for single-molecule force spectroscopy experiments (green and blue spheres). (b) In the experimental setup, a polystyrene bead is held in the trap that exerts force on the single molecule. The bead is covalently linked to 1.8 kbp of dsDNA, which is attached to biotin (green circle) at the other end. There is a noncovalent biotin/streptavidin interaction that then is linked to T4. CoA (blue circle) is covalently linked to T4 and another 50 bp of dsDNA that is attached to the polystyrene bead, which is held by suction. To see this figure in color, go online.