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Chemistry of Life Biology – S1 Video: http://viewpure.com/2Jgb_DpaQhM • Proteins • most diverse of all biological molecules • made by bonding amino acids together is specific orders • Amino acids • monomers (building blocks) of proteins • over 500 different AA are known • 20 AA are standard and make many different kinds of proteins • 9 are considered essential (must get from the diet) our body can’t make them • the shape determines the function of the protein *Failure to obtain enough of even 1 of the 10 essential amino acids, those that we cannot make, results in degradation of the body's proteins— muscle and so forth—to obtain the one amino acid that is needed. Unlike fat and starch, the human body does not store excess amino acids for later use— the amino acids must be in the food every day. 7 Classes of Proteins 1. Enzymes: help speed up chemical reactions (catalyst) without itself being changed (LOCK and KEY) • active site where substrate attaches Examples in our bodies • protease- breaks down proteins in meat, nuts, eggs,cheese • pepsin- breaks down proteins to peptides • peptidase- breaks down peptides to amino acids Enzymes/catalyst animation 2. Structural: build feathers, bones, cartilage, webs Keratin- makes up hair and nails •Collagen- makes up bone and cartilage 3. Transport: move molecules across cell membranes, • hemoglobin-moves oxygen to our body • insulin- controls glucose metabolism 4. contractile: provide muscular movement (actin and myosin- slide filament theory of contractions) 5. storage- (egg white) source of AA for embryo 6. defensive- antibodies, blood clotting 7. signal- hormones Denaturation- polypeptide chains unravel and lose their shape and function (frying an egg) clear proteins are denatured and they get white (useless)