BIOL 101 1st Edition Lecture 5 Outline of Last Lecture I. Why Carbon?II. IsomersIII. HydrocarbonsIV. Functional GroupsV. Chart of 6 Functional GroupsVI. Introduction to Macromolecules (Chapter 5)Outline of Current Lecture Proteins:I. StructureII. Amino AcidsIII. Polypeptide ChainsIV. Levels of Protein StructuresV. Protein FunctionCarbohydrates:I. StructureII. MonosaccharideCurrent LectureThese 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.Chapter 5 – Proteins Functional Group Quiz TuesdayI. Structurea. Polymers of amino acids (monomers)b. Connected by peptide bonds (know names of bond)c. Up to 50% of the dry weight of cells are proteinsd. Each has unique 3-D shape that determines functione. Protein functions:i. Structural supportii. Transport of molecules (ex. Hemoglobin)iii. Movement (ex. contract and expand muscles)iv. Biological catalysts  enzymesII. Amino Acidsa. Monomers of protein  20 common ones that makes up proteinsb. Classified by their “R” groupi. Nonpolarii. Polariii. Charged c. Know common shape of all amino acidsd. All have an asymmetric carbon – carbon has 4 different groups of atoms bonded to ite. Asymmetric carbon causes amino acids to have isometric forms (D and L forms)i. Only use L isomer to make proteinsIII. Polypeptide Chaina. Many amino acids joined together by peptide bondsb. Formed by peptide bondsc. Peptide bonds formed by dehydration synthesisd. Amino acids connected by peptide bonds have a repeating structuree. N-C-C-N-C-C-N-C-C  backbone of the proteinf. N-terminus  free amine group (one end) (NH2)g. C-terminus  free carboxyl group (other end) (CO2H)IV. Levels of Protein Structurea. Primary (1°)  sequence of amino acidsb. Secondary (2°) structure  repeating twisting and folding of the peptide backbone, caused by hydrogen bonding in backbone NOT due to R groupi. 2 types:1.∝ helix2.β-pleated sheetc. Tertiary (3°)structure  3-D shape due to interactions between R groupsi. Maintained by weak interactions:1. Hydrogen bonds2. Hydrophobic interactions between nonpolar “R” groups (interior of protein), whereas polar “R” groups are on the surface of protein interacting with H2Oii. Some proteins have covalent links that hold the 3-D shape together (“R” group)1. Ex. Cysteine (2 disulfide bonds)d. Quaternary (4°) structure  association of more than one polypeptide chain, not all proteins have this structure (some only have one polypeptide chain)i. Ex: collagen - 3 helical polypeptide chains intertwined into a triple helixii. Quaternary structure is held together by the same kind of forces as 3-D shape (mostly weak forces) V. Protein Functiona. Depends on 3-D shape (confirmation)b. Shape of protein allows it to recognize and bind to specific moleculesc. If it loses the shape, it also loses its’ ability to functiond. Loss of shape – denaturatione. Denatured proteins still have the primary structure (no broken peptide bonds) but it is no longer folded up in the 3-D shapeCarbohydratesI. Structurea. Sugars or polymers of sugari. Monosaccharide  simplest monomerii. Disaccharide  double sugarb. Energy source, storage, structural molecules, source of carbon to make other organic moleculesc. Bond  glycosidic bondd. Storage: starch, glycogene. Structural: celluloseII. Monosaccharidea. Contain C, H, O in a fixed ratio (CH2O)b. 3-7 carbons/sugar molecules i. 3C – trioseii. 5C – pentoseiii. 6C – hexosec. One hydroxyl (with exception of carboxyl carbon (C==O)d. Forms ring structuresi. Ex: glucose (hexose)III.IV. Disaccharidea. 2 monosaccharides joined by glycosidic bondsi. ex: maltose  two glucoses joined by dehydration synthesis (important disaccharide used in brewing beer)1. glycosidic bond joins C#1 of one glucose to C#4 of another lucoseii. glucose (6C) + galactose = lactoseiii. glucose (6C) + fructose (5C) = sucrose (table sugar)V. Polysaccharidea. Macromolecules formed by linking hundreds to thousands of monosaccharides by glycosidic bondsi. Storage polysaccharides – store energy1. Ex. Starch  (plants) polymer of glucose connected by α 1, 4 glycosidic bonds2.α glycosidic bonds  hydroxyl on C#1 is sticking down from the plane of the ring3.β glycosidic bonds  hydroxyl on C#1 is above the plane of the ring4. Ex. Glycogen  (animals) polymer of glucose, more branched than starch, stored in liver and muscleii. Structural Polysaccharides – forms structure1. Ex. Cellulose  (plants) plant cell walls, linear and unbranched polymer of glucose connected by β 1, 4 glucosidic bonds, polymer similar to starch but most organisms cannot hydrolyze glucose monomers from cellulose2. Ex. Chitin  structure polysaccharide of an amino structure, forms exoskeleton of arthropods, forms cell walls of some fungiThese notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a