BIOC 3560 Lecture Notes - Lecture 2: Van Der Waals Force, Disulfide, Quaternary

• School: University of Guelph
• Department: Biochemistry
• Course: BIOC 3560
• Professor: Manfred Brauer

Document Summary

Protein structure: primary structure: amino acid monomers are joined, forming polypeptide chains, secondary structure: polypeptide chains may form. Helices or pleated sheets: tertiary structure: polypeptides fold, forming specific shapes. Folds are stabilized by bonds and disulfide bridges. Determined by interaction of r groups through disulfide bonds, hydrogen bonds, ionic bonds, aggregation of hydrophobic side chains, and van der waals forces: quarternary structure: two+ polypeptides assemble to form larger protein molecules. The hypothetical molecule here is a tetramer, made up of four polypeptide subunits. This results from interaction of subunit via hydrophobic interactions. Van der waal forces, ionic bonds, and hydrogen bonds. Different representations can emphasize different properties of the protein structure. Function is influenced by interactions with other molecules. These interactions can be either stable or transient. A prosthetic group is a molecule that is permanently associated with a protein and required for its function.