BIOL 1411 1st Edition Lecture 3Outline of Last Lecture I. Atomic StructureII. BondingIII. Chemical ReactionsIV. WaterOutline of Current Lecture I. ProteinsII. CarbohydratesCurrent LecturePolymers- molecules of proteins, Carbohydrates, and nucleic acidsMonomers- make up polymers, covalently bondedMacromolecules- polymers with molecular weights exceeding 1,000Isomers- molecules that have the same chemical formula but arranged differentlyStructural isomers- differ in how atoms are joinedCis-trans isomers- involve a double bond between 2 carbon atoms, when carbons share 2 pairs of electronsOptical isomers- carbon atom has 4 different atoms or groups of atoms bondedCondensation reactions- results in formation of covalent bonds between monomersHydrolysis reactions- breakdown of polymers into monomers (releases energy)I. ProteinsProteins- polymers made up of 20 amino acidsPolypeptide chains- un-branched polymers of covalently bonded amino acidsDisulfide bridge- covalent bond helps determine how a polypeptide chain folds (2 cysteines interact)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.Peptide bond- carboxyl group of one amino acid reacts with the amino group of another forming bondPrimary structure- precise sequence of amino acids (linear)Secondary Structure- alpha helix and beta pleated sheet (hydrogen bonds)Tertiary Structure- 3D shape that arises from interactions (covalent, ionic, hydrogen bond, or hydrophobic) between R groupsQuaternary Structure- association of 2 or more polypeptides to form the functional proteinChaperones- proteins that help when proteins bind to wrong molecules after denaturation or when they are newly made and still unfoldedHeat shock proteins- general class of stress-induced chaperone proteinsN-terminus- starting proteinC-terminus- ending proteinDenatured- protein is heated; the secondary and tertiary structure is broken down, if cooled back down the protein returns to normal tertiary structure, demonstrating that the info to specify shape is in the primary structureHydrogen bonds- between N-H groups on 1 amino acid and C=O groupsProteins bond non-covalently with other cellular or extracellular molecules to perform their functionsBinding is very specificStructure of protein determines functionBetween protein and other molecules: ionic interactions occur between charged R groups, 2 non polar groups interact hydrophobically, hydrogen bonds form between 2 polar groups II. CarbohydratesGeneral formula: Cn(H2O)nMonosaccharaides- smallest sugars (3c to 6c)Disaccharides- 2 monosaccharaides linked by covalent bondsOligosaccharides- 3-20 monosaccharaidesPolysaccharides- hundreds or thousands of monosaccharaides (starch, glycogen,
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