BCH210H1 Lecture Notes - Lecture 1: Protein Folding, Sickle-Cell Disease, Red

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

Document Summary

Red colour cause by the fe heme complex. Tetramer: 2 alpha and two beta polypeptide chains. Signal change in amino acid (beta change) Caused by the replacement of the beta subunit from val to glu. Hemoglobin s (hb s) forms a long forms a long polymer changes the rbc"s shape. Amino acids determine the structure of the protein folding. Key to biological functions work as enzymes. Encoded by genes mutation in genes causes mutated protein lead to diseases. Certain enzymes and structure are produced in water. Hydrogen bonds (specific - based in dna use h bonds) Effects the shape of the protein structure. Hydrophobic (non polar) amino acids would be interior part of the globular protein. Hydrophilic (polar) amino acid would be on the exterior part of the globular protein. C and n bond between the base and ribose produces a nucleoside (adenosine) Metabolism is required a person to make and use atp at their own weight.