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Unformatted text preview: Macromolecule Function Monomers Construction of Polymers Structure Denature Process Differences Between Each Proteins Enzyme Catalysis- globular, facilitates chemical reactions Defense- globular, recognize foreign microbes and cancer cells Transport- globular, moves specific small molecules and ions example is hemoglobin Support- fibers, forms hair, nails, blood clots, cartilage Motion- muscles of two kinds: actin and myosin Regulation- hormones (intercellular messengers), cell surface receptors Storage- ion bonding to store iron and calcium Amino Acids- Contains carboxyl (-COOH) Amino group (-NH 2 ) Hydrogen atom (+H) Side Variable (R) 20 Common in 5 classes: 1. Nonpolar (-CH2 or –CH3) 2. Polar Uncharged (-H) 3. Charged (acids or bases) 4. Aromatic (organic ring with alt. single and double bonds) 5. Special- function Peptide Bond : Covalent bond that connects two amino acids; stiffness can determine shape of protein Polypeptide : long chains made up of amino acids linked by peptide bonds Determines the function Primary : determined by nucleotide sequence of gene Secondary : main chain polar groups form hydrogen bonds with each other: α helix (amino acids link with other further down chain)...
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This note was uploaded on 04/18/2008 for the course BIO 102 taught by Professor Haworth during the Spring '08 term at Marquette.
- Spring '08