BIOL 240 1st Edition Lecture 4 Outline of Last Lecture Carbon Compounds and LifeI. Life with carbona. Organic compoundb. Inorganic compoundII. Molecules with carbona. Most common pairingsb. HydrocarbonMacromoleculesI. Polymersa. Carbohydrates, proteins, nucleic acidsb. Dehydration reactionc. HydrolysisII. The diversity of polymersa. MacromoleculesIII. Carbohydratesa. Monosaccharideb. Polysaccharidei. Disaccharide1. Glycosidic linkageii. Storage polysaccharide1. Glucose polymers:iii. Insoluble fibers1. Alpha linkages vs. beta linkagesIV. Lipidsa. Fatsb. Phospholipidsc. SteroidsOutline of Current Lecture Continuation of MacromoleculesThese notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.I. Proteinsa. Functionsb. Monomer of proteins: amino acidsc. Polymer of amino acids (protein) can also be called a polypeptided. Protein structure and functioni. A functional proteinii. Four levels of protein structureiii. What determines protein structure?II. Nucleic Acidsa. Two types of nucleic acidsb. Polymer: DNA/RNAc. Monomer: nucleotidesIII. DNA in EvolutionCurrent LectureContinuation of MacromoleculesIV. Proteinsa. Make up 50% of the dry mass of most cellsb. Does the most in the cellc. Functions:i. Structural proteins: provide supportii. Storage proteins: provide amino acids for growthiii. Contractile proteins: help movementiv. Transport proteins: help transport substancesv. Enzymes: help chemical reactionsd. Monomer of proteins: amino acidsi. Organic molecule with carboxyl and amino groupsii. R groups (aka side groups): changes from one amino acid to another; convey different properties to the amino acids1. Nonpolar side chains: hydrophobic (no charge)2. Polar side chains: hydrophilic (partial charges)3. Electrically charged side chains (full charges)e. Polymer of amino acids (protein) can also be called a polypeptidei. Polypeptide bonds bind amino acidsii. Unique linear AA sequenceiii. Amino end: N-terminusiv. Carboxyl end: C-terminusf. Protein structure and functioni. A functional protein has:1. Correct sequencea. A protein’s sequence determines its structurei. Hydrophobic fold up in the proteinii. Hydrophilic fold to the outside of the protein2. Correct shapea. A protein’s structure determines its functioni. Allows it to bind to certain molecules (in a lock and key formation)ii. Four levels of protein structure1. Primary structure: string of amino acids2. Secondary structure: backbones bind to each other by hydrogen bondsa. Backbones: amino end and carboxyl endb. Can form alpha helix/beta pleated sheets3. Tertiary structure: side chains interact (R groups)a. Can be the end for some proteins4. Quaternary structure: several polypeptides togethera. Example: Collagen  holds cell togetheri. 40% if the protein in a human bodyb. Example: Hemoglobin  found in red blood cellsi. Carries/binds to oxygeniii. What determines protein structure?1. Physical and chemical conditionsa. Changes in pH, salt concentrations, temperature2. Denaturation: causes protein to change shape (will not function)3. Renaturation: return denatured proteins back to normalV. Nucleic Acidsa. Two types of nucleic acidsi. Deoxyribonucleic acid (DNA): inside nucleus of cellii. Ribonucleic acid (RNA)b. DNA  mRNA  Proteini. From nucleus to cytoplasmc. Polymer: DNA/RNAd. Monomer: nucleotidesi. Sugar (5-carbon), phosphate, nitrogenous base1. Basesa. Pyrimidinei. Cytosine (C)ii. Thymine (T, in DNA)iii. Uracil (U, in RNA)b. Purinei. Adenine (A)ii. Guanine (G)c. Pairings:i. C  Tii. A  Gd. Sugar groupsi. Deoxyribose (in DNA)  one less oxygenii. Ribose (in RNA)  one more oxygenVI. DNA in Evolutiona. DNA is passed from parents to offspringb. DNA differences in peoplec. Relatedness seen in DNA