Protein Modeling (11.29.10)

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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

Hydrophobic/Hydrophilic

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

intermolecular

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

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