BIOL 200 Lecture Notes - Lecture 2: Van Der Waals Force, Protein Structure, Biomaterial

• School: UBC
• Department: Biology
• Course: BIOL 200
• Professor: Vivienne Lam

Document Summary

Synthesis of new phospholipids synthesized (cytoplasmic face of er) by enzymes. Glycosylation (in lumen of golgi): enzymatic modification of organic molecule (especially protein) to carbohydrate. There are 2 leaflets on the membrane and the orientation of those leaflets remain constant. Non-covalent bonds between atoms in two r groups. Note: ( ) = not the main interactions for stabilization of the particular level but involved in overall structure. Match each property with the level(s) of protein structure: examples of this are alpha helices and beta-pleated sheets secondary, results from repetitive bonds between atoms in the peptide backbone. Secondary: can be altered when a protein is reversibly denatured. Secondary, tertiary, quaternary (anything with noncovalent bonds: results from covalent bonds formed between an amino group and a carboxyl group. Primary: results from covalent bonds between two s-containing r groups. Tertiary and quaternary: results from covalent and non-covalent interactions between r groups within one polypeptide chain. Tertiary: is also known as the protein sequence.