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.
User:John S. de Banzie/Globular Protein
From Proteopedia
(Difference between revisions)
m |
|||
| Line 1: | Line 1: | ||
| - | == | + | ==Simple Example of Globular Protein Structure== |
| - | <StructureSection load=' | + | <StructureSection load='1qvg' size='400' side='right' caption='U5 Spliceosomal protein, [[1qvg]]' scene='58/587846/Testrun/3'> |
| - | This | + | Most proteins are globular proteins. This page uses the human spliceosomal protein U5-15kD to illustrate some basic features of globular proteins. Specifically: |
| - | + | ||
| - | + | 1. Globular proteins are compact and rarely have internal cavities. | |
| + | 2. Globular protein structure is primarily stabilized by the hydrophobic interaction. | ||
| + | 3. Globular proteins have mixed secondary structure. | ||
| - | + | (U5-15kD is a component of the U5 small nuclear ribosomal protein particle (snRNP). This in turn is a component of the spliceosome, a macromolecule assembly involved in converting primary transcripts into functional mRNAs. U5-15kD was chosen for this page because it is small, but has the features necessary to illustrate the points being made.) | |
| - | = | + | The <scene name='58/587846/U5-15kd_sf/1'>space filling model</scene> of the protein shows that the protein is compact, globular, and has no signs of internal cavities. |
| - | = | + | <scene name='58/587846/U5-15kd_phobicity/1'>Colouring the hydrophilic and hydrophobic residues</scene> shows that the interior of the protein is primarily hydrophobic (red) and the exterior is primarily hydrophilic (blue). |
| - | + | The <scene name='58/587846/U5-15kd_ca/1'>cartoon view</scene> of the protein shows that the protein has mixed secondary structure. There are three segments of alpha-helix (magenta), six segments of beta-pleated sheet (gold), and some irregular regions (white). | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Revision as of 18:44, 31 May 2014
Simple Example of Globular Protein Structure
| |||||||||||
