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Chapter 5 Study Guide 4 major groups of macromolecules carbs, nucleic acids, proteins, lipids dehydration vs. hydrolysis what happens in each when each is used dehydration is used in polysaccharides, lipids, and proteins a water molecule is removed hydrolysis breaks a water molecule apart and its parts become attached to monomer. Breaks apart fats, proteins, and polysaccharides steroids have multiple rings, with functional groups sticking out chemical formulas and molecular structures for all carbs , lipids (3 types), proteins (primary and secondary structures) carbs have a CHO ratio of 1:2:1, can tell molecular structure by numerous –OH lipids have a CH ratio of 1:2, and only 2 oxygens, molecular structure has numerous C-H bonds protein molecular structure – look for amino and carboxyl functional groups monosaccharide, disaccharide, polysaccharide number of molecules examples of each type mono- 1 molecule, glucose, fructose di – 2 molecules, lactose poly – many, cellulose, starch, chitin starch vs. cellulose why can’t humans digest cellulose polymers of glucose starch stores energy, alpha glycosidic linkages cellulose used for structural purposes, beta glycosidic linkages can’t digest b/can’t break down beta glycosidic linkages facts about lipids insoluable in water makes components of cell membrane stores 2x as much energy as glucose triacylglycerol made of 3 fatty acids and a glycerol saturated fatty acid no C-C double bonds unsaturated fatty acid one or more C- C double bonds hydrogenation – what it does decreases# of C-C double bonds increases # of H atoms at room temp, goes from oil to solid saturated fatty acid vs. unsaturated fatty acid solid at room temp / liquid at room temp b/c double bonds make kinks in structure polypeptide polymer of amino acids parts of an amino acid amino group, carboxyl groups, H, central carbon, and R group what makes amino acids different from one another The R group, or side chain types of R groups ( polar, nonpolar, basic, acidic, hydrophobic, hydrophilic) Hydrophobic R groups contain mostly C and H peptide bonds – where formed formed between carboxyl of one amino acid and the amino group of the next amino acid, one molecule of water is removed during bond N terminus vs. C terminus N – side by amino group C- side by carboxyl group Bonds in primary, secondary, and tertiary structures Alpha helix, beta pleated sheets – where found When are the interactions of R groups important Purpose of disulfide bridges Primary structure – peptide bonds Secondary structure – hydrogen bonds, alpha helix, beta pleated sheets Tertiary – 3-D shape of fully folded polypeptide Disulfide bonds help maintain 3-D shape Interactions of R groups happen at tertiary level What happens to protein when 1 amino acid is changed It can change primary and tertiary structures, and biological activity Altering any of the structures can change the function of the protein Examples of protein molecules form 5.4 Hemoglobin Collegen Transthyretin lysozyme Denaturation – what is it, what structure does it affect A change in a protein’s 3-D shape or conformation due to disruption of H bonds, Ionic bonds, or disulfide bridges Chaperonins Molecules that insure the proper folding of a protein Function of RNA Function in the synthesis of protein Pats of a nucleotide 5 carbon sugar, nitrogenous base, phosphate group Purines vs. pryamidines Purines – adenine and guanine, 2 rings Pyramidiens – thymine, cytosine, uracil, 1 ring A-T G-C DNA bases vs. RNA bases DNA – A, T, G, C RNA – A, U, G, C Differences between DNA and RNA DNA - two strands, deoxyribose sugar, one less O than RNA RNA – one strand, ribose sugar What bonds hold the two sides of DNA together Hydrogen bonds