Chapter 14.1-14.4 Proteins Heather Bobber, Zoë Berkheimer, and Tyler Sterling 14.1: Functions of Proteins Most important biological compound Greek “proteios” – “of first importance” Functions Structure Skin, bones, hair, and nails Ex. Collagen and Keratin Catalysis Enzymes that speed up reactions in living organisms Movement Muscles are made of myosin and actin Functions (continued) Transport Transport nutrients in cells Ex. Hemoglobin carries oxygen in blood from the lungs to the cells Hormones Some proteins are hormones Ex. Insulin, erythropoietin, and human growth hormones Protection Antibodies and fibrinogen which is involved in blood clotting Storage Proteins store materials Ex. Ferritin stores iron in the liver Functions (continued) Regulation Controls the expression of genes and manufacturing of proteins in cells One cell has 9000 different proteins while the human body has 100,000. There are 2 types of proteins Fibrous proteins: insoluble in water and are used for structural purposes. Globular proteins: soluble in water and are used for nonstructural purposes. 14.2: Amino Acids Proteins are chains of amino acids Amino Acid- An organic compound containing an amino group and a carboxyl group In nature there are 20 common amino acids called alpha amino acids Amino Acids (continued) There are 4 groups of chains based on their polarity Non-polar, polar but neutral, acidic, and basic Non-polar is hydrophobic The other three are hydrophilic Most amino acids are L-isomers and D-amino acids are rare in nature. 14.3: Zwitterions Zwitterions: compounds with a positive charge on one atom and a negative charge on another atom Zwitter – German “hybrid” Amino acids are zwitterions Ionic compounds Solids, high melting points Fairly soluble in water Zwitterions Continued Amino acids are negative ions at high pH and positive at low pH Isoelectric point – pH at which the sample of amino acid or protein has an equal number of positive and negative charges 14.4: Characteristics of Amino Acids The side chain gives unique properties to amino acids Example: Cysteine can be easily dimerized to cystine Some amino acids have acidic or basic properties Glutamic acid and Aspartic acid have carboxylic acid groups on side chain Histidine, lysine, and arginine have basic side chains Phenylalanine, tryptophan, and tyrosine have aromatic rings in their side chains, making them key precursors to neurotransmitter Tryptophan is converted to serotonin Tyrosine is converted to adrenaline