Scleroprotein
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Scleroproteins are one of the two main classes of protein tertiary structure (the other being globular proteins).
They are also called fibrous proteins.
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[edit] Characteristics
They form long protein filaments, rod- or wire-like shapes. They are usually inert structural or storage proteins. They are generally water-insoluble and are found as an aggregate due to hydrophobic R groups that stick out of the molecule. The amino acid sequences they are made from often have limited residues with repeats. These can form unusual secondary structures, e.g. collagen triple helix. The structures often contain 'cross-links' between chains, for example cys-cys disulfide bonds between keratin chains.
Globular proteins tend to denature more easily than fibrous proteins.
[edit] Functions
They usually play a role which is protective or supportive.[1]
They are usually used to construct connective tissues, tendons, bone matrix and muscle fiber.
Attempts at artificial synthesis have been made.[2]
[edit] Examples
Examples of include keratins, collagens and elastins.
Another example is fibroin.[3]
[edit] See also
[edit] References
- ^ scleroprotein at Dorland's Medical Dictionary
- ^ 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. PMID 9680195. http://peds.oxfordjournals.org/cgi/pmidlookup?view=long&pmid=9680195.
- ^ "Fibrous Protein Homepage". http://web.chemistry.gatech.edu/~williams/bCourse_Information/6521/protein/fibrous/fibrous.html. Retrieved on 2008-11-26.
[edit] External links
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