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Chapter 5 The Structure and Function of Large Biological Molecules Overview: The Molecules of Life • All living things are made up of four classes of large biological molecules: carbohydrates, lipids, proteins, and nucleic acids • Within cells, small organic molecules are joined together to form larger molecules • Macromolecules are large molecules composed of thousands of covalently connected atoms • Molecular structure and function are inseparable Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Macromolecules are polymers, built from monomers • A polymer is a long molecule consisting of many similar building blocks • These small building-block molecules are called monomers • Three of the four classes of life’s organic molecules are polymers: – Carbohydrates – Proteins – Nucleic acids Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-2a HO Reaction to build or breakdown 1 2 3 H Short polymer HO H Unlinked monomer Dehydration removes a water molecule, forming a new bond H2O Synthesis HO 1 2 3 4 H Longer polymer (a) Dehydration reaction in the synthesis of a polymer Fig. 5-2b Reaction to build or breakdown HO 1 2 3 4 Hydrolysis adds a water molecule, breaking a bond H H2O Breakdown/degredation HO 1 2 3 (b) Hydrolysis of a polymer H HO H Carbohydrates serve as fuel and building material • Carbohydrates include sugars and the polymers of sugars • The simplest carbohydrates are monosaccharides, or single sugars • Carbohydrate macromolecules are polysaccharides, polymers composed of many sugar building blocks Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Sugars • Monosaccharides have molecular formulas that are usually multiples of CH2O • Glucose (C6H12O6) is the most common monosaccharide • Monosaccharides are classified by – The location of the carbonyl group (as aldose or ketose) – The number of carbons in the carbon skeleton Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-3 Trioses (C3H6O3) Pentoses (C5H10O5) Hexoses (C6H12O6) Glyceraldehyde Examples of Monosaccharides Ribose Glucose Galactose Dihydroxyacetone Ribulose Fructose Fig. 5-4 Various ways to present macromolecules (a) Linear and ring forms (b) Abbreviated ring structure Fig. 5-5 Examples of synthesis 1–4 glycosidic linkage Glucose Glucose Maltose (a) Dehydration reaction in the synthesis of maltose 1–2 glycosidic linkage Glucose Fructose (b) Dehydration reaction in the synthesis of sucrose Sucrose Polysaccharides • Polysaccharides, the polymers of sugars, have storage and structural roles • The structure and function of a polysaccharide are determined by its sugar monomers and the positions of glycosidic linkages Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-6 Two examples of Polysaccharides Chloroplast Mitochondria Glycogen granules Starch 0.5 µm 1 µm Glycogen Amylose Amylopectin (a) Starch: a plant polysaccharide (b) Glycogen: an animal polysaccharide Fig. 5-7 Chemistry of bond directs processing of Molecule (a) and glucose ring structures Glucose (b) Starch: 1–4 linkage of glucose monomers Glucose (b) Cellulose: 1–4 linkage of glucose monomers Fig. 5-8 Cell walls Cellulose microfibrils in a plant cell wall Microfibril 10 µm 0.5 µm Cellulose molecules b Glucose monomer Fig. 5-10 (a) The structure of the chitin monomer. (b) Chitin forms the exoskeleton of arthropods. (c) Chitin is used to make a strong and flexible surgical thread. Lipids are a diverse group of hydrophobic molecules • Lipids are the one class of large biological molecules that do not form polymers • The unifying feature of lipids is having little or no affinity for water • Lipids are hydrophobic because they consist mostly of hydrocarbons, which form nonpolar covalent bonds • The most biologically important lipids are fats, phospholipids, and steroids Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fats • Fats are constructed from two types of smaller molecules: glycerol and fatty acids • Glycerol is a three-carbon alcohol with a hydroxyl group attached to each carbon • A fatty acid consists of a carboxyl group attached to a long carbon skeleton Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-11a Fatty acid (palmitic acid) Glycerol (a) Dehydration reaction in the synthesis of a fat Fig. 5-11b Ester linkage (b) Fat molecule (triacylglycerol) Fig. 5-12a Structural formula of a saturated fat molecule Stearic acid, a saturated fatty acid (a) Saturated fat Fig. 5-12b Structural formula of an unsaturated fat molecule Oleic acid, an unsaturated fatty acid (b) Unsaturated fat cis double bond causes bending Phospholipids • In a phospholipid, two fatty acids and a phosphate group are attached to glycerol • The two fatty acid tails are hydrophobic, but the phosphate group and its attachments form a hydrophilic head Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Hydrophobic tails Hydrophilic head Fig. 5-13 (a) Structural formula Choline Phosphate Glycerol Fatty acids Hydrophilic head Hydrophobic tails (b) Space-filling model (c) Phospholipid symbol Fig. 5-14 Hydrophilic head Hydrophobic tail WATER WATER Steroids • Steroids are lipids characterized by a carbon skeleton consisting of four fused rings • Cholesterol, an important steroid, is a component in animal cell membranes • Although cholesterol is essential in animals, high levels in the blood may contribute to cardiovascular disease Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-15 Proteins have many structures, resulting in a wide range of functions • Proteins account for more than 50% of the dry mass of most cells • Protein functions include structural support, storage, transport, cellular communications, movement, and defense against foreign substances Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Table 5-1 • Enzymes are a type of protein that acts as a catalyst to speed up chemical reactions • Enzymes can perform their functions repeatedly, functioning as workhorses that carry out the processes of life Animation: Enzymes Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-16 Breakdown of a Disaccharide Substrate (sucrose) Glucose OH Fructose HO Enzyme (sucrase) H2O Polypeptides • Polypeptides are polymers built from the same set of 20 amino acids • A protein consists of one or more polypeptides Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Amino Acid Monomers • Amino acids are organic molecules with carboxyl and amino groups • Amino acids differ in their properties due to differing side chains, called R groups Amino group Carboxyl group Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-UN5 Fig. 5-17a Nonpolar Glycine (Gly or G) Methionine (Met or M) Alanine (Ala or A) Valine (Val or V) Phenylalanine (Phe or F) Leucine (Leu or L) Tryptophan (Trp or W) Isoleucine (Ile or I) Proline (Pro or P) Fig. 5-17b Polar Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y) Asparagine Glutamine (Asn or N) (Gln or Q) Fig. 5-17c Electrically charged Acidic Aspartic acid Glutamic acid (Glu or E) (Asp or D) Basic Lysine (Lys or K) Arginine (Arg or R) Histidine (His or H) Amino Acid Polymers • Amino acids are linked by peptide bonds • A polypeptide is a polymer of amino acids • Polypeptides range in length from a few to more than a thousand monomers • Each polypeptide has a unique linear sequence of amino acids Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-18 Peptide bond (a) Side chains Peptide bond Backbone (b) Amino end (N-terminus) Carboxyl end (C-terminus) Fig. 5-20 Protein from flu virus Antibody protein Protein Structure and Function The sequence of amino acids determines a protein’s threedimensional structure A protein’s structure determines its function • Primary structure, the sequence of amino acids in a protein, is like the order of letters in a long word • Primary structure is determined by inherited genetic information Animation: Primary Protein Structure Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-21 Four Levels of Protein Structure Primary Structure Secondary Structure pleated sheet +H N 3 Amino end Examples of amino acid subunits helix Tertiary Structure Quaternary Structure Fig. 5-21d Abdominal glands of the spider secrete silk fibers made of a structural protein containing pleated sheets. The radiating strands, made of dry silk fibers, maintain the shape of the web. The spiral strands (capture strands) are elastic, stretching in response to wind, rain, and the touch of insects. Fig. 5-21e Tertiary Structure Quaternary Structure Fig. 5-21f Hydrophobic interactions and van der Waals interactions Polypeptide backbone Hydrogen bond Disulfide bridge Ionic bond Fig. 5-21g Polypeptide chain Chains Iron Heme Chains Hemoglobin Collagen Sickle-Cell Disease: A Change in Primary Structure • A slight change in primary structure can affect a protein’s structure and ability to function • Sickle-cell disease, an inherited blood disorder, results from a single amino acid substitution in the protein hemoglobin Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-22a Normal hemoglobin Primary structure Val His Leu Thr Pro Glu Glu 1 2 Secondary and tertiary structures 3 4 5 6 7 subunit Quaternary structure Normal hemoglobin (top view) Function Molecules do not associate with one another; each carries oxygen. Fig. 5-22b Sickle-cell hemoglobin Primary structure Secondary and tertiary structures Val His Leu Thr Pro Val Glu 1 2 3 Exposed hydrophobic region Quaternary structure Sickle-cell hemoglobin Function Molecules interact with one another and crystallize into a fiber; capacity to carry oxygen is greatly reduced. 4 5 6 7 subunit Fig. 5-22c 10 µm Normal red blood cells are full of individual hemoglobin molecules, each carrying oxygen. 10 µm Fibers of abnormal hemoglobin deform red blood cell into sickle shape. What Determines Protein Structure? • In addition to primary structure, physical and chemical conditions can affect structure • Alterations in pH, salt concentration, temperature, or other environmental factors can cause a protein to unravel • This loss of a protein’s native structure is called denaturation • A denatured protein is biologically inactive Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-23 Denaturation Normal protein Renaturation Denatured protein Nucleic acids store and transmit hereditary information • The amino acid sequence of a polypeptide is programmed by a unit of inheritance called a gene • Genes are made of DNA, a nucleic acid Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings The Roles of Nucleic Acids • There are two types of nucleic acids: – Deoxyribonucleic acid (DNA) – Ribonucleic acid (RNA) • DNA provides directions for its own replication • DNA directs synthesis of messenger RNA (mRNA) and, through mRNA, controls protein synthesis • Protein synthesis occurs in ribosomes Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-26-3 DNA 1 Synthesis of mRNA in the nucleus mRNA NUCLEUS CYTOPLASM mRNA 2 Movement of mRNA into cytoplasm via nuclear pore Ribosome 3 Synthesis of protein Polypeptide Amino acids Fig. 5-27ab 5' end The Structure of Nucleic Acids 5'C 3'C Nucleoside Nitrogenous base 5'C Phosphate group 5'C 3'C (b) Nucleotide 3' end (a) Polynucleotide, or nucleic acid 3'C Sugar (pentose) Fig. 5-27c-1 Nitrogenous bases Pyrimidines Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA) Purines Adenine (A) Guanine (G) (c) Nucleoside components: nitrogenous bases Fig. 5-UN6 Fig. 5-27c-2 Sugars Deoxyribose (in DNA) Ribose (in RNA) (c) Nucleoside components: sugars Nucleotide Monomers • Nucleoside = nitrogenous base + sugar • There are two families of nitrogenous bases: – Pyrimidines (cytosine, thymine, and uracil) have a single six-membered ring – Purines (adenine and guanine) have a sixmembered ring fused to a five-membered ring • In DNA, the sugar is deoxyribose; in RNA, the sugar is ribose • Nucleotide = nucleoside + phosphate group Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Nucleotide Polymers • Nucleotide polymers are linked together to build a polynucleotide • Adjacent nucleotides are joined by covalent bonds that form between the –OH group on the 3 carbon of one nucleotide and the phosphate on the 5 carbon on the next • These links create a backbone of sugarphosphate units with nitrogenous bases as appendages • The sequence of bases along a DNA or mRNA polymer is unique for each gene Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings The DNA Double Helix • A DNA molecule has two polynucleotides spiraling around an imaginary axis, forming a double helix • In the DNA double helix, the two backbones run in opposite 5 → 3 directions from each other, an arrangement referred to as antiparallel • One DNA molecule includes many genes • The nitrogenous bases in DNA pair up and form hydrogen bonds: adenine (A) always with thymine (T), and guanine (G) always with cytosine (C) Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-28 5' end 3' end Sugar-phosphate backbones Base pair (joined by hydrogen bonding) Old strands Nucleotide about to be added to a new strand 3' end 5' end New strands 5' end 3' end 5' end 3' end Fig. 5-UN10 Fig. 5-UN8 Fig. 5-UN2a Fig. 5-UN2b Fig. 5-UN9