This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox Reserved 1446
From Proteopedia
(Difference between revisions)
| Line 10: | Line 10: | ||
The structure of the fibers typically form quaternary beta-sheet structures. The quaternary structure creates a larger group of polypeptides and proteins, which is stabilized by hydrogen bonds, disulfide-bridges, and salt-bridges. | The structure of the fibers typically form quaternary beta-sheet structures. The quaternary structure creates a larger group of polypeptides and proteins, which is stabilized by hydrogen bonds, disulfide-bridges, and salt-bridges. | ||
== Function == | == Function == | ||
| - | + | Amyloids have numerous functions for all organisms: | |
| + | -Spider silk is formed by amyloids | ||
| + | -Increase cell adhesion on the top of Fungi to have stronger bonding | ||
| + | -Peptides and proteins are stored in the endocrine system of humans as amyloids | ||
| + | -Malaria uses amyloids as a coat protein | ||
| + | -Gas vesicles (that aid in buoyancy) of aquatic archaea and eubacteria | ||
== Disease == | == Disease == | ||
Revision as of 20:07, 30 April 2018
| This Sandbox is Reserved from Jan 22 through May 22, 2018 for use in the course Biochemistry II taught by Jason Telford at the Maryville University, St. Louis, Missouri, USA. This reservation includes Sandbox Reserved 1446 through Sandbox Reserved 1455. |
To get started:
More help: Help:Editing |
Amyloid
| |||||||||||

