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UW-Madison BIOLOGY 151 - Macromolecules

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Bio 151 1nd Edition Lecture 2 Outline of Last Lecture I. Water II. BondsIII. Importance of waterIV. Polymers/MonomersCurrent Lecture- Carbohydrates: composed of polysaccharides (many sugars)o Diversity comes from: Linkages and extent of branching: - Starch vs. celluloseo Monomers: glucose (6 sugars)o Linkages in starch are alpha form: exposes –OH functional groupso Linkages in cellulose are beta glucose monomers  functional groups are flipped (ribbons/bundle)rigid, linear molecule- Chitin: polymer of N-containing sugars  used to make exoskeletons of insects Roles for carbohydrates: o Structural: cellulose (plants), chitin (fungi, animals)o Energy: starch, glycogen Sugar names (for monomers): end in –oseo Ei. 5C: ribose, deoxyribose; 6C: glucose, fructose, galactose- Lipids: made up of glycerol and fatty acids; to make a lipid: glycerol backbone, fatty acid (non polar)=react together via dehydration reaction polaro Forms of lipids: Fat: glycerol + 3 fatty acids = triacylglycerol - INCREDIBLY HYDROPHOBIC Phospholipids: (2 fatty acids + glycerol + phosphate[hydrophilic, polar])- Duel nature: hydrophilic head, hydrophobic tail.o In water, assembles into micelle: self assembles, no energy, heads out-tails in.These 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.- Proteins: made up of monomers called amino acids (amine + carboxyl acid)o Amino acids: Chemical diversity comes from R groups (20 different R groups for amino acids) Amino acids are connected by peptide bonds: covalent bonds between groupso Levels of protein structure: Primary structure: sequence of amino acids Secondary structure: interactions between amino acids close by- Alpha helix- Beta pleat sheet: amino acids interact with another amino acid chain Tertiary structure: 3D shape that alpha and beta assume; interactions between different regions of the protein  3D shape- Includes hydrophobic, van der waals, interacting ionic bonds, disulfide bridge (covalent bond between sulfides that form) Quaternary structure: involves complex and interactions between individual proteins- Denature protein: protein+ (high temp, salt, pH extremes) garbage- Denaturation: refold denatured protein, reverse


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