Foods and Nutrition 1021 Lecture Notes - Lecture 6: Phenylalanine Hydroxylase, Toxic Heavy Metal, Basal Metabolic Rate

• School: Western University
• Department: Foods and Nutrition
• Course: Foods and Nutrition 1021
• Professor: Noelle Martin

Document Summary

Side chain: creates a unique chemical structure, differentiates one aa from another, makes aa differ in size/shape/electrical charge join together via peptide bonds to form proteins in the body. Peptide bonds: chemical bond formed between the amine group end of one aa and the acid group end of the next. Each aa carries an electrical charge that attracts or repels various ends of each aa resulting in different shapes and sizes. Examples: enzymes act as protein catalysts, globular hemoglobin carries o2 and fe, collagen makes up tendons and ligaments. Cannot be synthesized at all or are present in insufficient amounts to meet physiological needs. Isoleucine: leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine. 11 dispensable aa: alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline serine tyrosine. Normally non-essential aa, but must be supplied by the diet when the body cannot meet its needs tyrosine from phenylalanine becomes essential in phenylketonuria (pku) Altered to make another compound (ex. niacin)