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Updated: Jul 20, 2026

Combining Single-molecule Manipulation and Imaging for the Study of Protein-DNA Interactions
Published on: August 27, 2014
Bioengineered flagella protein nanotubes with cysteine loops: self-assembly and manipulation in an optical trap
Mudalige Thilak Kumara1, Narayanan Srividya, Subra Muralidharan
1Department of Chemistry and Nanotechnology Research and Computation Center, Western Michigan University, Kalamazoo, Michigan 49008-5410, USA.
Abstract:
An E. coli flagellin protein, termed FliTrx, was investigated for use as a novel form of self-assembling protein nanotube. This protein was genetically engineered to display constrained peptide loops with a series of different thiol, cationic, anionic, and imidazole functional groups. "Cys-loop" thiol variants consisting of 6 and 12 cysteine residues were isolated in the form of disulfide-linked nanotube bundles, a novel nanomaterial. Bundles were characterized by fluorescence microscopy, transmission electron microscopy, and optical trapping.
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