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A scleroprotein forms long protein filaments, which are shaped like rods or wires. Scleroprotein are structural proteins or storage proteins that are typically inert and water-insoluble. A scleroprotein occurs as an aggregate due to hydrophobic side chains that protrude from the molecule.
A scleroprotein's peptide sequence often has limited residues with repeats; these can form unusual secondary structures, such as a collagen helix. The structures often feature cross-links between chains (e.g., cys-cys disulfide bonds between keratin chains).
Miroshnikov et al. (1998) are among the researchers who have attempted to synthesize fibrous proteins.
- Miroshnikov KA, Marusich EI, Cerritelli ME, et al. (April 1998). "Engineering trimeric fibrous proteins based on bacteriophage T4 adhesins". Protein Eng. 11 (4): 329–32. doi:10.1093/protein/11.4.329. PMID 9680195.