Amyloid: Difference between revisions
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Amyloid fibrils are protein structures that are misfolded due to mutations, error in covalent modification, and other unknown causes. These proteins are insoluble and usually clump together to form mass known as ''plaques''. The fibrils clump together as they are made up of ß sheets that are able to pack tightly. <ref>Lodish et al (2013). Molecular Cell Biology. New York: W.H Freeman and Company. p76-77.</ref><br> <br> These defective protein structures are often associated with many neurodegenerative disorders such as Parkinson's and Alzheimer's diseases as well as prion diseases. However, some bacteria use these fibres for distributing their spores and infecting host tissues. <ref>Alberts et al (2014). Essential Cell Biology. 4th ed. New York: Garland Publications. p132-134.</ref> | Amyloid fibrils are protein structures that are misfolded due to mutations, error in covalent modification, and other unknown causes. These proteins are insoluble and usually clump together to form mass known as ''plaques''. The fibrils clump together as they are made up of ß sheets that are able to pack tightly. <ref>Lodish et al (2013). Molecular Cell Biology. 7th Ed. New York: W.H Freeman and Company. p76-77.</ref><br> <br> These defective protein structures are often associated with many neurodegenerative disorders such as Parkinson's and Alzheimer's diseases as well as prion diseases. However, some bacteria use these fibres for distributing their spores and infecting host tissues. <ref>Alberts et al (2014). Essential Cell Biology. 4th ed. New York: Garland Publications. p132-134.</ref> | ||
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Revision as of 07:05, 21 November 2014
Amyloid fibrils are protein structures that are misfolded due to mutations, error in covalent modification, and other unknown causes. These proteins are insoluble and usually clump together to form mass known as plaques. The fibrils clump together as they are made up of ß sheets that are able to pack tightly. [1]
These defective protein structures are often associated with many neurodegenerative disorders such as Parkinson's and Alzheimer's diseases as well as prion diseases. However, some bacteria use these fibres for distributing their spores and infecting host tissues. [2]
References