BCH210H1 Lecture Notes - Lecture 5: Globular Protein, Alpha Helix, Pancreatic Ribonuclease

• School: UTSG
• Department: Biochemical Engineering and Applied Chemistry
• Course: BCH210H1
• Professor: Wright

Document Summary

Single actin subunit globular shape, can bind to atp and polymerize. Monomers can form together and created an actin filament. Then when atp is catalyst, it hydrolysis and produces adp. Many enzymes with active site bind substrates and catalyze reactions. Consist largely of secondary structure elements (helix, sheets, turns) Fe-heme binds oxygen, protein stores it until required for metabolic oxidation. 153 aa: 121/153 in alpha helices purpose is to form heme pockets. 8 connected helix segments which form heme pocket. Helices folds via turns (turn contain pro) Heme prosthetic group that allows the heme fe bind. Has a couple of his residue that helps stabilize the heme fe in the myoglobin. Enzyme that cuts rna, but not dna. Taco-shape molecule with the active site in a crevice running across the molecule. Small protein with beta sheets and alpha helix. Has 4 disulfide bonds (common in secreted proteins) Active site located by binding an inhibitor.