Fibrous protein: Difference between revisions
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{{Technical|date=August 2010|section=Biomolecular structure}} |
{{Technical|date=August 2010|section=Biomolecular structure}} |
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[[Image:Collagentriplehelix.png|thumb|right|79px|Tropocollagen [[triple helix]]]] |
[[Image:Collagentriplehelix.png|thumb|right|79px|Tropocollagen [[triple helix]]]] |
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'''Scleroproteins''', or '''fibrous proteins''',<ref name="Saad 1994">{{cite book|last1=Saad|first1=Mohamed|title=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.|date=Oct 1994|publisher=PhD Thesis, Université Joseph Fourier Grenoble I|pages=1–221|url=https://drive.google.com/open?id=0B3L_EN9hIuFTTkhuN2lrWEU4RDQ&authuser=0 |doi= 10.13140/2.1.4776.7844}}</ref> constitute one of the three main topologies of [[protein]]s, alongside [[globular protein]]s and [[membrane protein]]s. There are many scleroprotein [[protein superfamilies|superfamilies]] including [[ |
'''Scleroproteins''', or '''fibrous proteins''',<ref name="Saad 1994">{{cite book|last1=Saad|first1=Mohamed|title=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.|date=Oct 1994|publisher=PhD Thesis, Université Joseph Fourier Grenoble I|pages=1–221|url=https://drive.google.com/open?id=0B3L_EN9hIuFTTkhuN2lrWEU4RDQ&authuser=0 |doi= 10.13140/2.1.4776.7844}}</ref> constitute one of the three main topologies of [[protein]]s, alongside [[globular protein]]s and [[membrane protein]]s. There are many scleroprotein [[protein superfamilies|superfamilies]] including [[keratin]], [[collagen]], [[elastin]], and [[fibroin]]. The roles of such proteins include protection and support, forming [[connective tissue]], [[tendon]]s, [[Bone#Matrix|bone matrices]], and [[muscle fiber]]. |
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==Biomolecular structure== |
==Biomolecular structure== |
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Revision as of 12:04, 16 June 2015
 | This article may be too technical for most readers to understand. (August 2010) |
Scleroproteins, or fibrous proteins,[1] constitute one of the three main topologies of proteins, alongside globular proteins and membrane proteins. 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. 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).
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.[2]
References
- ^ 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.
- ^ 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.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link)
External links
- Scleroproteins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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