Key Concepts
Most macromolecules are polymers, built from monomers 5.2 Carbohydrates serve as fuel and building material 5.3 Lipids are a diverse group of hydrophobic molecules 5.4 Proteins have many structures, resulting in a wide range of functions 5.5 Nucleic acids store and transmit hereditary information 5.1

Chapter Review
Smaller organic molecules are joined togeth .er to form carbohydrates, lipids, proteins, and nuc Ieic acids. These molecules, many of which are giant r nacromolecules, represent another level in the hiera rchy of biological organization, and their functions derive from their complex and unique architectures. 5.1 Most macromolecules are polymers s built from monomers Polymers are chainlike molecules fan ned from the linking together of many similar or il dentical small molecules, called monomers. Synthesis and Breakdown of Polunu ere Monomers are joined by condensation reactions (or dehydration reactions), in which one monomer prc rvides a hydroxyl group (-OR) and the other contrib .utes a hydrogen (- H) to release a water molecule. W ith an input of energy and the help of enzym,es, a ( zovalent bond between the monomers is formed. Hydrolysis is the breaking (J If bonds between monomers through the addition 0. f water molecules. A hydroxyl group is joined to one monomer while a hydrogen is bonded with the otl rer. Enzymes also control hydrolysis.
Functions Energy, raw materials, energy storage,

~ :Framework
The central ideas of this chapter are that molecular function relates to molecular structure and that the diversity of molecular structure is the basis for the diversity of life. Combining a small number of monomers or subunits into unique sequences and three-dimensional structures creates a huge variety of macromolecules. The table below briefly summarizes the major characteristics of the four classes of macromolecules.

Class Carbohydrates Proteins Nucleic acids Lipids

Monomers Monosaccharides Amino acids Nucleotides Glycerol and fatty acids phospholipids; steroids (do not form polymers)

:uctural compounds

Enzymes, transport, movement, receptor s, defense, structure Heredity, code for amino add sequence fats; Energy storage, membranes, hormones


The seemingly endless variety of polymer :'S arises from the essentially infinite number of possibili ties:in the sequencing and arrangement of these basic bui ilding blocks. most monosacchar 'ides form (e) _ OH H GLUCOSE OH H GLUCOSE OH Sucrose.26 U. is a polyrru er made of glucose molecules joined by 1-4 linkages tha t give starch a helical shape. Cellulose. Then draw the resulting maltose molecule with its 1-4 glycosidic linkage (between the number 1 carbon of the first glucose and the number 4 carbon of the second).. Chitin is a structural polysaccharide formed from glucose monomers with a nitrogen-containing group and found in the exoskeleton of arthropods and the cell walls of many fungi. You can recoqi nize a monosaccharide by its multiple (a) 9 'roups and its one (b) group. fill in the blant csto review the structure of monosaccharides.2 Cal :bohydrates serve as fuel and buiJ lding material Carbohj zdrates include sugars and their polymers. arides. nit 01 ne: The Chemistry of Life Diversi ty of Polymers Macromolecules are constructed 1fronn about 40 to 50 cornmon monomers and a few ran zr molecules. Polysaccharides Polysaccharides are storage or structural macromolecule ~s made from a few hundred to a few thousand monosacc harides. and fungi) have enzymes that can digest cellulose. Sugar molecules' may be enantiomers due to the spatial arrangeme -nt of parts around asymmetric carbons. Starch. Only a few organisms (some bacteria. trioses. a. It differs from starch by the configuration of the ring form of glucose and the resulting geometry of the glycosidic bonds. as their energy storage form. microorganisms. a highly branched polymer of glucose. glucose. Monosaccharides serve also as the raw materials fo: r synthesis of other organic molecules and as monomer 's that are synthesized into disaccharides or polysacch. INTERAC nvs QUESTION 5. In aqueous solutions. In a plant cell wall.2 . A glycosidic linkage is a covalent bond formed by a dehydration reaction between two mono: saccharides. Animals produce glycogen. with hexoses (C6H1206). 5. Glucose is broken down to yield energy in cellular respiration. Enzymes that digest the IT linkages of starch are unable to hydrolyze the 13 linkages of cellulose. a (d) .1 Circlethe atoms of these two glucose molecules that will be removed by a dehydration reaction. is a disaccharide consisting of a glucose and a frue :tose molecule. II INTERACTIVE QUESTION 5. Whose location determines whether the sugar is an (e) or. is the most abundant organic compound on Earth. the major component of plant cell walls. hydrogen bonds between hydroxyl groups hold parallel cellulose molecules together to form strong microfibrils. nd pentoses found most commonly. a storage molecule in plants. or table t mga'f. Most animals have enzyr nes to hydrolyze plant starch into ]v1ALTOSE . Sugars Monosaccharides have the general formula of (CH2C ))n' The number of these units forming a sugar varies fn Jm three to seven.

~. Triglyceride is another name for fats. . The phosphate head of this molecule is hydrophilic and water soluble. . The unique structure of phospholipids makes them ideal constituents of cell membranes. Fats are excellent energy storage molecules. whereas the two fatty acid chains are hydrophobic. and label the hydrophilic head and hydrophobic tail of one of the phospholipids. Most animal fats are saturated and solid at room temperature. glyceroL A fatty acid consists of a long hydrocarbon chain with a carboxyl group at one end.:. glucose with nitrogen group 5. and steroids are a diverse assemblage of macromolecules that are classed together as lipids based on their hydrophobic behavior.Chapter 5: The Structure and Function of Macromolecules 27 iii INTERACTIVE QUESTION 5. phospholipids. The nonpolar hydrocarbons make a fat hydrophobic. Arranged in a bilayer. .3 Fill in the following concept map that summarizes this section on carbohydrates. A triacylglycerol. a bond that forms between a hydroxyl and a carboxyl group. Fatty acids with double bonds in their carbon skeletons are called unsaturated fatty acids.. The cis double bonds create a kink in the hydrocarbon chain and prevent fat molecules that contain unsaturated fatty acids from packing closely together and becoming solidified at room temperature. the hydrophilic heads face toward the aqueous solutions inside and outside the cell. to which other small molecules may be attached.3 Lipids are a diverse group of hydrophobic molecules Fats. III INTERACTIVE QU ESTION 5. made of fat storage cells. Cholesterol is an important steroid that is a common component of animal cellmembranes and a precursor for other steroids. and the hydrophobic tails mingle in the center of the membrane.4 Sketch a section of a phospholipid bilayer of a membrane. consists of three fatty acid molecules. Saturated fatty adds have no double bonds in their carbon skeletons. Diets rich in saturated fats and in "trans fats" made in the process of hydrogenating vegetable oils have been linked to cardiovascular disease.j. each linked to glycerol by an ester linkage. The fats of plants and fish are generally unsaturated and are called oils. f Phospholipids Phospholipids consist of a glycerol linked to two fatty acids and a negatively charged phosphate group. Lipids do not form polymers. including many hormones . general formula ~ function as [_J c. Adipose tissue. ·f Steroids Steroids are a class of lipids distinguished by four connected carbon rings with various functional groups attached. or fat. also cushions organs and insulates the body. Fats Fats are composed of fatty acids attached to the three-carbon alcohol. containing twice the energy reserves of carbohydrates such as starch.

determining their amino acid sequences. Polypeptides A polypeptide is a polymer of amino acids. and then overlapping the sequences of small fragments created with different agents to reconstruct the whole polypeptide. an amino group. Most of these steps are now automated. =-==-. IIIlI INTERACTIVE QUESTION 5. Which ____ of these amino acids has a polar R group? a nonpolar R group? _ c. a carthe boxyl group. A peptide bond links the amino group of one amino acid with the carboxyl group of another.28 Unit One: The Chemistry of Life III INTERACTIVE . Sanger determined the primary structure of insulin through the laborious process of hydrolyzing the protein into small peptide chains. Amino acids are composed of an asymmetric carbon <Called a carbon) bonded to a hydrogen. What does this molecule segment represent? Note the N-C~C-N-C-C sequence. b. At the pH in a cell. The R group confers the unique physical and chemical properties of each amino acid.. A protein consists of one or more polypeptide chains folded into a specific three-dimensional shape or conformation . resulting in a wide range of functions Proteins are central to almost every function of life. and a variable side chain called the R group. . Side chains may be either nonpolar and hydrophobic. g forms a ---.4 Proteins have many structures./" '=pooed of rr. QU ESTION 5.5 your understanding of lipids Fill in this concept map to help you organize are a. enzymatic proteins selectively speed up the chemical reactions of a cell.6 a. A polypeptide chain has a free amino group at one end and a free carboxyl group at the other. the amino and carboxyl groups are usually ionized. hydrophilic head hydrophobic tail 5. Polypeptides vary in length from a few to a thousand or more amino acids.. or polar or charged (acidic or basic) and thus hydrophilic. In the late 1940s and early '50s..-. Draw the amino acids alanine (R group-CH3) and serine (R group-CH20H) and then show how a dehydration reaction will form a peptide bond between them. molecules with is a are '" charged.. -N-C-C-N-C-C-N-C-CI II HO I II HO I II H0 7 I 7 I 7 I Protein Conformation and Function Proteins have unique three-dimensional shapes created by the twisting . As catalysts. i.

create your own map to help you organize the key concepts you have learned about proteins. The amino acid sequences of more than 100. coupled with computer modeling and graphics. _ CHz-CHz- r----II CHZ. . One version of a protein concept map is included in the answer section. temperature. Interactions between the various side chains (R groups) of the constituent amino acids produce a protein's tertiary structure. Try to include the concepts of structure and function and look for crosslinks on your map. Quaternary structure occurs in proteins that are composed of more than one polypeptide chain.----_ d. label the types of interactions that are shown. Protein conformation is dependent upon the interactions among the amino acids making up the polypeptide chain and usually arises spontaneously as soon as the protein is synthesized in the cell. which results from its sequence of amino acids. called disulfide bridges. III INTERACTIVE QUESTION 5. Primary structure is the unique. Secondary structure involves the coiling or folding of the polypeptide backbone. enables it to recognize and bind to other molecules.NH3 + -OJ'!"_C-CHz o .000proteins have been determined. Hydrophobic interactions between nonpolar side groups clumped in the center of the molecule due to their repulsion by water.7 In the following diagram of a portion of a polypeptide. What does that indicate about a protein's conformation? Ii INTERACTIVE QUESTION 5. Even a slight deviation from the sequence of amino acids can severely affect a protein's function by altering the protein's conformation. perhaps by providing a sheltered environment. A p pleated sheet is also held by repeated hydrogen bonds along the polypeptide backbone. What level of structure are these interactions producing? b. and the protein may denature. may occur between the sulfhydryl side groups of cysteine monomers that have been brought close together by the folding of the polypeptide.8 a. or other aspects of the environment. Why would a change in pH cause a protein to denature? b. The individual polypeptide subunits are held together in a precise structural arrangement. An a helix is a coil produced by hydrogen bonding between every fourth amino acid. chaperone proteins that assist other proteins during the folding process.9 Now that you have gained more experience with concept maps. Researchers have developed methods for following a protein through its intermediate states on the way to its final form and have discovered chaperonins. and ionic bonds between negatively and positively charged side chains produce the stable and unique shape of the protein. Why would transfer to a nonpolar organic solvent (such as ether) cause denaturation? c. biochemists have established the threedimensional shape of thousands of these molecules.Chapter 5: The Structure and Function of Macromolecules 29 or folding of one or more polypeptide chains. A denatured protein may re-form to its functional shape when returned to its normal environment. This secondary structure forms when regions of the polypeptide chain lie parallel to each other.. salt concentration. Strong covalent bonds. The interactions that create and maintain secondary and tertiary structure can be disrupted by changes in pH. hydrogen bonds between polar side chains. stabilized by hydrogen bonds between the electronegative oxygen of one peptide bond and the weakly positive hydrogen attached to the nitrogen of another peptide bond. A substitution of only one of the 146 amino acids in the primary structure of hemoglobin causes sickle-cell disease. but remember that the real value is in the thinking process you must go through to create your own map. The unique conformation of a protein. losing its native conformation and thus its function. Using the technique of X-ray crystallography. genetically coded sequence of amino acids within a protein. van der Waals interactions among those nonpolar side chains. !II INTERACTIVE QU ESTION 5.

!I!!! INTERACTIVE The Structure of Nucleic Acids Nucleic acids.5 Nucleic acids store and transmit hereditary information Genes are the units of inheritance that determine the primary stru. uracil is only in RNA In DNA}the pentose is deoxyribose.12 Take the time to create a concept map that summarizes what you have just reviewed about nucleic acids. the sequences of nitrogenous bases on the two strands of DNA are complementary. This "molecular genealogy" provides evidence of evolutionary relationships. guanine always pairs with cytosine. also called polynucleotides. Thymine is only in DNA. Isthis a DNA or RNA nucleotide? Show the flow of genetic information in a cell. The nitrogenous bases extend from this backbone of repeating sugarphosphate units. One version of a map on nucleic acids is included in the answer section. Pyrimidines. The Roles of Nucleic Acids DNA. thymine (T). More closely related species have a larger proportion of their DNA and proteins in common. DNA and Proteins as Tape Measures of Evolution Genes form the hereditary link between generations.10 c. --~-~----~---The DNA Double Helix DNA molecules consist of two chains of polynucleotides spiraling around an imaginary axis in a double helix.cture of proteins. Purines. Indicate with an arrow where the phosphate group of the next nucleotide would attach to build a polynucleotide. Because of this specificbase-pairing property. are characterized by six-membered rings of carbon and nitrogen atoms. which consists of two sugar-phosphate backbones on the outside of the helix with their nitrogenous bases pairing and hydrogenbonding together in the inside. are polymers of nucleotidesmonomers that consist of a pentose (five-carbon sugar) covalently bonded to a phosphate group and a nitrogenous base. Compare your map with that of a study partner or explain it to a friend. adenine (A) and guanine (G)} add a fivemembered ring to the pyrimidine ring. Nucleotides are linked together into a polynucleotide by phosphodiester linkages. The two chains run in opposite 5' to 3' directions. DNA can replicate itself and precisely copy the genes of inheritance. b. Closely related members of the same species share many common DNA sequences and proteins. which join the phosphate of one nucleotide with the sugar of the next. The instructions coded in DNA are transcribed to RNA. Nucleic acids are polymers that carry and transmit this code. QU ESTION 5. the ultimate enactors of the genetic program. Refer to Figures 5. ribonucleic acid. Label the three parts of this nucleotide. In a eukaryotic cell. is the genetic material that is inherited from one generation to the next and is reproduced in each cell of an organism.30 Unit One: The Chemistry of Life 5. deoxyribonucleic add.11 a. A monomer without the phosphate group is called a nucleoside. The polymer has two distinct ends: a 5' end with a phosphate attached to a 5' carbon and a 3' end with a hydroxyl group on a 3' carbon. which directs the synthesis of proteins. The unique sequence of bases in a gene codes for the specific amino acid sequence of a protein. an arrangement called antiparallel. Number the carbons of the pentose sugar.27 in your textbook to help you visualize polynucleotides and the double helix of DNA. Is this a purine or a pyrimidine? !S INTERACTIVE QUESTION 5. ~ INTERACTIVE QUESTION 5. induding cytosine (C). DNA resides in the nucleus and messenger RNA carries the instructions for protein synthesis to ribosomes located in the cytoplasm. in RNA it is ribose. Thus. . Adenine pairs only with thymine.26 and 5. In 1953Watson and Crick first proposed this double-helix arrangement. There are two families of nitrogenous bases. and uracil (U).

monomer of a protein 7.Chapter 5: The Structure and Function of Macromolecules 31 The Theme of Emergent Properties in the Chemistry of Life: A Review At each stage in the hierarchy of levels from atoms through macromolecules.~ J~qil~' lJo~reoge~ K _.= many (polysaccharide: many monosaccharides joined together) / tri. I I I g. most nonpolar (hydrophobic) molecule c. Then match the chemical formulae with their description.. -lyse = break (hydrolysis: breaking chemical bonds by adding water) macro. Answers may be used more than once. --------- 0- the formulas shown on the right.. molecule that is a purine 6. I II / IIIII H H H H H a fat ___ ___ ___ ____ ____ ____ ____ ~ 2. \ ~ H H3N+ C _c4'f' H t ~ ~ . . ___ ~ 1.= part (polymer: a chain made from smaller organic molecules) mono..= together (condensation reaction: a reaction in which two molecules become covalently bonded to each other through the loss of a small molecule. molecule that would be attached to other monomers by a peptide bond H b.C-NH '-'N/ d._.= single. I N/'" hC' C-N I ~CH HC:-. molecules or groups that would combine to form a nucleotide ~ 4. we have seen that novel properties arise with increasing structural organization.#O C R-C-OH H-c-OH H f.= large (macromolecule: a large molecule) meres. -sacchar = sugar (monosaccharide: simplest type of sugar) poly.= sweet (glycogen: a polysaccharide sugar used to store energy in animals) hydro.= three (triacylglycerol: three fatty acids linked to one glycerol molecule) = di- r $frtiCf~J.- _ I I 0 1.= water. groups that would be joined by phosphodiester bonds 8.. 2. usually water) two (disaccharide: two monosaccharides joined together) glyco. Describe the four structural levels in the conformation of a protein. con. Identify the type of monomer or group shown by '\ a. molecules that would combine to form o H H H H H HO " C-C-C I -CI -C-C-etc. 0- II I I H-C-OH I H H-C-OH I H-C-OH -o-p-o0 I II II~r OH OR e. molecules that are carbohydrates 5. H. NH2 ~ 3.

in the monomers involved. a double helix. It differs from starch because of the configuration of glucose and the geometry of the glycosidic linkage. 9. unsaturated fats. 4. c. d. and peptide bonds are disrupted. It may be an aldose or a ketose. b. c. starch. Three molecules of the fatty acid in question 8 are joined to a molecule of glycerol (C3Hs03). e. saturated. c. hydrophobic interactions. b. involves the removal of a water molecule. e. It loses its secondary and tertiary structures. Its hydrogen bonds. The Chemistry of Life ifest~our·Knoiyleug¢· MATCHING: Match the molecule with its type of molecule. b. It becomes irreversibly insoluble and precipitates. d. e. The rxhelix of proteins is a. Plants store most of their energy as a. may involve all of the above. enzyme 9. It has one carbonyl and four hydroxyl groups. nucleic acid 2. RNA c. 6. It has the formula CSH1ZOS' d. C48H9606' 4. Few organisms have enzymes that hydrolyze its glycosidic linkages. chitin MULTIPLE CHOICE: Choose the one best answer. part of the tertiary structure and is stabilized by disulfide bridges. e. protein D. d. 3. cellulose. b. Which of the following is not true of a pentose? a. c. cholesterol 3. lipid C. a complementary sequence to messenger RNA. creates bonds between amino acids in the formation of a peptide chain. It is the most abundant organic compound on Earth. C48H9809. 5. C51HI0Z()8' d. stabilized by hydrogen bonds and commonly found in fibrous proteins. 1. glycogen A. It can occur in a ring structure. Polymerization is a process that a. triacylglycerol 8. e. Disaccharides can differ from each other in all of the following ways except a. e. C51HI04()9' . d. b. . b. 8. ionic bonds. e. c. d. glycogen. found in some regions of globular proteins and stabilized by hydrophobic interactions. c. cellulose ____ 10. in the number of their monosaccharides. requires a condensation or dehydration reaction. a gene 7. A fatty acid that has the formula C1J-i3zOz is a. hemoglobin 6. The resulting molecule has the formula a. branched. It may be hydrogen-bonded to neighboring cellulose molecules to form microfibrils. b. in their structural formulas. C51H98()6. 1. as enantiomers. d. Which of the following is not true of cellulose? a. part of a steroid molecule. 2. hydrophilic. links the sugar of one nucleotide with the phosphate of the next. collagen 5. disulfide bridges. b. unsaturated. e. in the location of their glycosidic linkage. 7. It loses its primary structure. carbohydrate B.32 Unit One. It can be found in nucleic acids. sucrose. c. Its monomers are glucose with nitrogencontaining appendages. b. e. c. It hydrolyzes into component amino acids. What happens when a protein denatures? a. d.

b.2 d. c. the sequence of nucleotides in DNA. ClOHzoOlO c. ester linkages between the carboxyl group of one nucleotide and the hydroxyl group on the ribose of the next 16. Which of these molecules would provide the most energy (kcal/ g) when eaten? a. OH 3.pO H CH2 yC" ~2 I I tr I ~+ -. they can convert cellulose to starch and then hydrolyze starch to glucose. folds stabilized by hydrogen bonds between segments of the polypeptide backbone. glycogen d. c. What is the molecular formula for this disaccharide? a. e. GCCTAA b. C12H24012 e. both 2 and 4 b. chitin amino acid polypeptide (tripeptide) nucleotide protein 18. C12H24013 15. CGGATT d. I 1 I[ 2 3 I I[ I. they can produce the enzymes that break the ~ linkages between glucose molecules. e. Which of the following hydrophobic molecule? a. Cows can derive nutrients from cellulose because a.Chapter 5: The Structure and Function of Macromo~ecules 33 ~ pleated sheets are characterized by a. hydrogen bonds between adjacent cellulose molecules. which was determined by the sequence of nucleotides in RNA d. 3 e. their intestinal tract contains termites. 1 c. C6H1206 b. fat e. disulfide bridges between cysteine amino acids. covalent bonds between the sugar of one nu-deotide and the phosphate of the next e. e. d. protein What determines the sequence of the amino acids in a particular protein? a. Sucrose is made from joining a glucose and a fructose molecule in a dehydration reaction. TAAGCC . d. disulfide bridges between cysteine amino acids d. ionic attractions between phosphate groups c. one of their stomachs contains bacteria that can hydrolyze the bonds of cellulose.4 19. the three-dimensional shape of the protein 14. ATTCGG e. b. N-C-C-N-C-C-N-C-C / I II II CH2 H CH2 OH 0 H 0 H 0 H . which produce enzymes to hydrolyze cellulose. d. hydrogen bonds between complementary nitrogenous base pairs b. the sequence of nucleotides in RNA. How are the nucleotide monomers connected to form a polynucleotide? a. c. they chew and rechew their cud so that cellulose fibers are finally broken down. chitin e. C12H220n d. b. the sequence of RNAnucleotides making up the ribosome e.CGGAUU c. parallel regions of the polypeptide chain held together by hydrophobic interactions. What is the best description of this molecule? H H -. starch c. glucose would be the most 17. nucleotide c. glucose b. amino acid d. its primary structure b. which was determined by the sequence of nucleotides in the gene for that protein c. cholesterol b. Which number(s) in the molecule in question 17 refer(s) to a peptide bond? a. If the nudeotide sequence of one strand of a DNA helix is GCCTAA what would be the sequence on the complementary strand? a. membrane sheets composed of phospholipids.

b. 21. polynucleotides e. fats that are derived from animal sources and are associated with cardiovascular disease d. Proteins that assist the proper folding of newly synthesized proteins are called _ . catalyst for metabolic reactions c. cellulose b. glycogen and cellulose d. Which of the following is not a function performed by proteins? a. Cytosine always pairs with 3. monkeys evolved from humans. The man who determined the amino acid sequence of insulin was _ 2. unsaturated fats c. unsaturated fatty acids 22. Proteins with more than one polypeptide chain have structure. phospholipids e. fats made from cholesterol that are components of plaques in the walls of blood vessels c. What are trans fats? a. c. Hydrophobic as well as hydrophillic interactions would be important for which of the following types of molecules? a. indicatingthat a. the two groups first appeared on Earth at about the same time. polyunsaturated fats produced by removing H from fatty acids and forming cis double bonds 24. Membranes are composed of a bilayer of 9. the two groups belong to the same species. d. Monkeys and humans share many of the same DNA sequences and have similar proteins. hydrogenated vegetable oils that have been identified with health risks b. the two groups share a relatively recent common ancestor. Adenine and guanine are _ _ 4. humans evolved from monkeys. 7. The carbohydrate energy storagemolecule of animalsis _ 8. proteins b. The insoluble fiber listed on food packages consists primarily of _ 10. signals and receptors e. A pentose joined to a nitrogenous base and a phosphate group is called a _ 5. e.34 Unit One: The Chemistry of Life 20. protection against disease d. The conformation of a protein is determined by its 6. chitin c. cholesterol d. Which of the following would be the major component of the cell membrane of a fungus? a. all of the above 23. primary component of cell membranes FILL IN THE BLANKS 1. fats that contain trans double bonds and may contribute to atherosclerosis e. transport of oxygen in blood b.

aldose d. saturated: no C=C. starch . all possible C-H bonds g. cell membrane i steroids j. monomers e. or other ions. serine's R group is polar. a polypeptide backbone 5.7 a. energy compounds d. A protein in an organic solvent would turn inside out as the hydrophilic regions became clustered on the inside of the molecule and the hydrophobic regions interacted with the nonpolar solvent. (CH20)n 5. carbon skeletons. cell membrane component (cholesterol). c. hydrophobic and van der Waals interactions c. thereby disrupting the hydrogen bonding and ionic bonds that maintain protein shape. disulfide bridge d. alanine's R group is nonpolar c. chitin 5. b. glycerol d.3 a. H-N-C-C-~ I II H0 alanine OH H CH3 H CH3 OH H CH2 -N-C-C-OH H0 serine I c. hydroxyl b. rings MALTOSE 5. glycosidic linkages f. polysaccharides h. fatty acids e. disaccharides g. 11 H-N-C-C-N-C-C-OH H0 dipeptide I I I H CH2 I I I I II H0 II b. ketose e. hydrogen bond b. fats. The return to its functional shape indicates that a protein's conformation is intrinsically determined by its primary structure-the sequence of its amino acids.1 a.8 a.CHAPTER 5: THE STRUCTURE AND FUNCTION OF MACROMOLECULES iii INTERACTIVE QU ESTIONS 5. hormones 5.. unsaturated: C=C bonds f. carbonyl c. glycogen i. OH-. ionic bond These interactions between R groups produce tertiary structure. monosaccharides b. 5. triacylglycerides I -------.2 5. A change in pH alters the availability of H+. phospholipids c.k. phosphate group h. cellulose 1. animals j.6 II~II a.4 a. Hydrophilic head Hydrophobic tail .5 b.

.12 NUCLEIC ACIDS . m protems .9 ~ ~ are polymers7 of I iROTEINS """ function depends on I I I conf~rmation ~ joined by. disulfide bridges several polypeptide subunits hemoglobin. Nitrogenous base b.. DNA Phosphate group OH H 32 Attachment site ~eoxyribose for phosphate of next nucleotide 5.~~. ~ pleated sheet I hydrogen I maybe L R group contributes to hydrophobic.11 a.::h sequen~ ~ 1--__ -' bonder to ~ determmes is (l.10 DNA ---+ RNA ---+ Protein 5. Hbonds.. charged. membrane proteins myosin in muscles 5. van dcr Waals interactions. (acidic. lS~. ionic bonds. basic) hydrogen bonds within polypeptide backbone hydrophobic. pyrimidine c. consist of IS provides -.Lr------~ay are polymers of linked by I ~ be . code for amino acids . polar.5.__---. helix.

a 17. c 20. c 12. The tertiary structure involves interactions between the side chains of amino acids and produces a characteristic three-dimensional shape for a protein. ~yrine) ~ b.". quaternary glycogen phospholipids cellulose chaperonins (amino acid sequence) c. c 8. 24. B 8. genetically coded sequence of amino acids in a polypeptide chain. b 7.0 6. 6. 8. e 2.SUGGESTED ANSWERS TO STRUCTURE YOUR KNOWLEDGE 1. Sanger guanine purines nucleotide primary structure 6.. e. ANSWERS TO TEST YOUR KNOWLEDGE Matching: 1. c 7. a 7. purine (adenine) glycerol phosphate group pentose (ribose) sugar (triose) 5. 10. d 2. 22. 23. c 6. A . g. a 4. c 18. C 2. f. c 1. f 8. b 21. 2. 5. b 14. 1. A 11. A 4. 4. 7. d 10. Quaternary structure occurs in proteins composed of more than one p~lypeptide chain.1'a. stabilized by hydrogen bonds along the polypeptide backbone. c 15. The secondary structure involves the coiling (ex helix) or folding (13 pleated sheet) of the protein. The primary structure of a protein is the specific. a nitrogenous base. C 5. e 5. a 9. b. 3. D 1. d a d e 2. b . e. d. fatty acid Fill in the Blanks: F. b 19. .Multiple Choice: 16. C 9. B 3. 9. d 13. d 10. c 3.

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