Scleroprotein

Tropocollagen triple helix

Scleroproteins or fibrous proteins[1] constitute one of the three main types of proteins (alongside globular and membrane proteins).[2] There are many scleroprotein superfamilies including keratin, collagen, elastin, and fibroin. The roles of such proteins include protection and support, forming connective tissue, tendons, bone matrices, and muscle fiber.

Biomolecular structure

A scleroprotein forms long protein filaments, which are shaped like rods or wires. Scleroproteins 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).

Scleroproteins tend not to denature as easily as globular proteins.

Miroshnikov et al. (1998) are among the researchers who have attempted to synthesize fibrous proteins.[3]

References

  1. ↑ Saad, Mohamed (Oct 1994). Low resolution structure and packing investigations of collagen crystalline domains in tendon using Synchrotron Radiation X-rays, Structure factors determination, evaluation of Isomorphous Replacement methods and other modeling. PhD Thesis, Université Joseph Fourier Grenoble I. pp. 1–221. doi:10.13140/2.1.4776.7844.
  2. ↑ Andreeva, A (2014). "SCOP2 prototype: a new approach to protein structure mining". Nucleic Acids Res. 42: D310–4. doi:10.1093/nar/gkt1242. PMC 3964979. PMID 24293656.
  3. ↑ 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.


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