BCH 2333 Lecture Notes - Lecture 12: Protein Structure, Enzyme, Trypsin

• School: University of Ottawa
• Department: Biochemistry
• Course: BCH 2333
• Professor: Christopher Boddy

Document Summary

Ligands: what is being bound by the protein. Small molecules (amino acids, sugars, atp), other proteins, dna/rna. Binds to the iron in the heme group in the hemoglobin to form a protein-ligand complex. Chemistry: enzyme: protein that binds ligands and does chemistry, ex. Hiv protease normally binds to an unfolded protein sequence. Function: bind to antigens to generate immune response. Comes from equilibrium between p-l complex and free ligand (l) + free protein (l) Nb: sometimes ligand is referred to as s (substrate) or i (inhibitor) Nb: sometimes protein is referred to as e (enzyme) Kd is a concentration and has units of mol/l (m) Kd gives the concentration of ligand that saturates 50% of the sites: if 50% of p is bound to l, the [p] = [p-l] > therefore kd = [l] Almost all binding sites are saturated if the ligand concentration is 10 kd.