12 terms

Protein Modeling (11.29.10)

A brief review of protein structure and function.
Primary structure
linear; list of amino acids
Secondary structure
3-D; list of amino acids with alpha helices and beta sheets added
Tertiary structure
3-D; as seen on Jmol
Strongest individual bonds to weakest individual bonds
Disulfide bridge - Ionic bonds - Hydrophobic/Hydrophilic - Hydrogen bonds - Dipole-Dipole Interactions - Van der Waals attractions
Disulfide bridge
-S-S-; between cysteine residues; covalent; intramolecular
Ionic bonds
basic residues take a + charge, acidic residues take a - charge: basic residues and acidic residues are attracted to each other
intermolecular; different amino acids have an affinity for either water or oil
Hydrogen bonds
intermolecular; hydrogens bond because with such a small atomic radius, hydrogen can easily bond two larger amino acids
Dipole-Dipole Interactions
Van der Waals attractions
intermolecular; random electrostatic attractions; appear and disappear constantly; large, flat, close; help proteins stay together (significant in polymers, not normally)
Quaternary structure
more than one protein chain comes together
Pluripotent stem cells
stem cells that can become all the cell types that are found in an organism, but not the embryonic components of the trophoblast and placenta; can be used in research and medical treatment