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 1376
From Proteopedia
(Difference between revisions)
| Line 9: | Line 9: | ||
== Structural highlights == | == Structural highlights == | ||
| - | The 5xn9 protein derives its function primarily from | + | The 5xn9 protein derives its function primarily from several key sites. The first are the <scene name='77/777696/Beta_barrel/1'>beta barrels</scene>, two large beta-sheets that coil to form a barrel-like structure that allows hydrophobic residues to form unusual networks of hydrogen bonds. Beta barrels are commonly seen in membrane proteins and often contain alternating residues of hydrophobic and hydrophilic amino acids, as can be seen <scene name='77/777696/Hydrophobic/1'>here</scene> with hydrophobic regions in red and hydrophilic regions in turquoise. The particular beta barrel on 5xn9 is very similar to that of '''fatty acid binding proteins (FABPs)'''. |
Revision as of 21:41, 22 February 2018
SAHS protein from Ramazzottius varieornatus
| |||||||||||
