Sandbox GGC9: Difference between revisions
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This is a default text for your page '''Sandbox GGC9'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Sandbox GGC9'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI doi: 10.1128/JVI.00555-16</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. <ref name="prion">http://www.hopkinsmedicine.org/healthlibrary/conditions/nervous_system_disorders/prion_diseases_134,56/ | You may include any references to papers as in: the use of JSmol in Proteopedia <ref name="structure"/>DOI doi: 10.1128/JVI.00555-16</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. <ref name="prion">http://www.hopkinsmedicine.org/healthlibrary/conditions/nervous_system_disorders/prion_diseases_134,56/ | ||
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== Function == | == Function == | ||
Prions are proteins with compromised folds in their structure. They can convert a normal protein into a replicate of their own abnormal form. This can lead to deadly degenerative diseases of the brain. Studies have shown that prions are linked to Alzheimer's and Parkinson's disease. | Prions are proteins with compromised folds in their structure. They can convert a normal protein into a replicate of their own abnormal form. This can lead to deadly degenerative diseases of the brain. Studies have shown that prions are linked to Alzheimer's and Parkinson's disease. | ||