University:
Kentucky State University
Course:
CHE 315 | Biochemistry
Academic year:

2023
Views:

16

Pages:

67
Author:

Lyric Morgan

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 • Macromolecules are large molecules composed of thousands of covalently connected atoms • Molecular structure and function are inseparable Concept 5.1: 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 The Synthesis and Breakdown of Polymers • A dehydration reaction occurs when two monomers bond together through the loss of a water molecule • Polymers are disassembled to monomers by hydrolysis, a reaction that is essentially the reverse of the dehydration reaction Animation: Polymers Figure 5.2 (a) Dehydration reaction: synthesizing a polymer 1 2 3 Short polymer Unlinked monomer Dehydration removes a water molecule, forming a new bond. 1 2 3 4 Longer polymer (b) Hydrolysis: breaking down a polymer 1 2 3 Hydrolysis adds a water molecule, breaking a bond. 1 2 3 4 Concept 5.2: 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 Sugars • Monosaccharides have molecular formulas that are usually multiples of CH2O (1:2:1) • 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 Figure 5.3 Aldoses (Aldehyde Sugars) Ketoses (Ketone Sugars) Trioses: 3-carbon sugars (C3H6O3) Glyceraldehyde Dihydroxyacetone Pentoses: 5-carbon sugars (C5H10O5) Ribose Ribulose Hexoses: 6-carbon sugars (C6H12O6) Glucose Galactose Fructose • A disaccharide is formed when a dehydration reaction joins two monosaccharides • This covalent bond is called a glycosidic linkage Animation: Disaccharide Figure 5.5 1–4 glycosidic 1 linkage 4 Glucose Glucose Maltose (a) Dehydration reaction in the synthesis of maltose 1–2 glycosidic 1 linkage 2 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 Storage Polysaccharides • Starch, a storage polysaccharide of plants, consists entirely of glucose monomers • Plants store surplus starch as granules within chloroplasts and other plastids • The simplest form of starch is amylose Figure 5.6 Chloroplast Starch granules Amylopectin Amylose (a) Starch: 1 m a plant polysaccharide Mitochondria Glycogen granules Glycogen (b) Glycogen: 0.5 m an animal polysaccharide • Glycogen is a storage polysaccharide in animals • Humans and other vertebrates store glycogen mainly in liver and muscle cells Structural Polysaccharides • The polysaccharide cellulose is a major component of the tough wall of plant cells • Like starch, cellulose is a polymer of glucose, but the glycosidic linkages differ • The difference is based on two ring forms for glucose: alpha () and beta () Animation: Polysaccharides Figure 5.7 (a)  and  glucose ring structures 4 1 4  Glucose  Glucose 1 4 (b) Starch: 1–4 linkage of  glucose monomers 1 1 4 (c) Cellulose: 1–4 linkage of  glucose monomers Figure 5.8 Cellulose microfibrils in a plant cell wall Cell wall Microfibril 10 m 0.5 m Cellulose molecules  Glucose monomer • Enzymes that digest starch by hydrolyzing  linkages can’t hydrolyze  linkages in cellulose • Cellulose in human food passes through the digestive tract as insoluble fiber • Some microbes use enzymes to digest cellulose • Many herbivores, from cows to termites, have symbiotic relationships with these microbes • Chitin, another structural polysaccharide, is found in the exoskeleton of arthropods • Chitin also provides structural support for the cell walls of many fungi Figure 5.9 The structure of the chitin monomer Chitin forms the exoskeleton of arthropods. Chitin is used to make a strong and flexible surgical thread that decomposes after the wound or incision heals. Concept 5.3: 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 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 Figure 5.10 Fatty acid (in this case, palmitic acid) Glycerol (a) One of three dehydration reactions in the synthesis of a fat Ester linkage (b) Fat molecule (triacylglycerol) • Fatty acids vary in length (number of carbons) and in the number and locations of double bonds • Saturated fatty acids have the maximum number of hydrogen atoms possible and no double bonds • Unsaturated fatty acids have one or more double bonds Animation: Fats Figure 5.11 (a) Saturated fat Structural formula of a saturated fat molecule Space-filling model of stearic acid, a saturated fatty acid (b) Unsaturated fat Structural formula of an unsaturated fat molecule Space-filling model of oleic acid, an unsaturated fatty acid Cis double bond causes bending. • Fats made from saturated fatty acids are called saturated fats, and are solid at room temperature • Most animal fats are saturated • Fats made from unsaturated fatty acids are called unsaturated fats or oils, and are liquid at room temperature • Plant fats and fish fats are usually unsaturated • A diet rich in saturated fats may contribute to cardiovascular disease through plaque deposits • Hydrogenation is the process of converting unsaturated fats to saturated fats by adding hydrogen • Hydrogenating vegetable oils also creates unsaturated fats with trans double bonds • These trans fats may contribute more than saturated fats to cardiovascular disease • The major function of fats is energy storage • Fat also serves as insulation, vitamin carriers, and hunger suppressors. • Humans and other mammals store their fat in adipose cells • Adipose tissue also cushions vital organs and insulates the body 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 Hydrophobic tails Hydrophilic head Figure 5.12 Choline Phosphate Glycerol Fatty acids Hydrophilic head Hydrophobic tails (a) Structural formula (b) Space-filling model (c) Phospholipid symbol • When phospholipids are added to water, they self-assemble into a bilayer, with the hydrophobic tails pointing toward the interior • The structure of phospholipids results in a bilayer arrangement found in cell membranes • Phospholipids are the major component of all cell membranes Figure 5.13 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 Figure 5.14 Concept 5.4: Proteins include a diversity of 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 Figure 5.15-a Enzymatic proteins Defensive proteins Function: Selective acceleration of chemical reactions Example: Digestive enzymes catalyze the hydrolysis of bonds in food molecules. Function: Protection against disease Example: Antibodies inactivate and help destroy viruses and bacteria. Antibodies Enzyme Virus Bacterium Storage proteins Transport proteins Function: Storage of amino acids Function: Transport of substances Examples: Hemoglobin, the iron-containing protein of vertebrate blood, transports oxygen from the lungs to other parts of the body. Other proteins transport molecules across cell membranes. Examples: Casein, the protein of milk, is the major source of amino acids for baby mammals. Plants have storage proteins in their seeds. Ovalbumin is the protein of egg white, used as an amino acid source for the developing embryo. Transport protein Ovalbumin Amino acids for embryo Cell membrane • 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 Figure 5.15-b Hormonal proteins Receptor proteins Function: Coordination of an organism’s activities Example: Insulin, a hormone secreted by the pancreas, causes other tissues to take up glucose, thus regulating blood sugar concentration Function: Response of cell to chemical stimuli Example: Receptors built into the membrane of a nerve cell detect signaling molecules released by other nerve cells. High blood sugar Insulin secreted Normal blood sugar Receptor protein Signaling molecules Contractile and motor proteins Structural proteins Function: Movement Examples: Motor proteins are responsible for the undulations of cilia and flagella. Actin and myosin proteins are responsible for the contraction of muscles. Function: Support Examples: Keratin is the protein of hair, horns, feathers, and other skin appendages. Insects and spiders use silk fibers to make their cocoons and webs, respectively. Collagen and elastin proteins provide a fibrous framework in animal connective tissues. Actin Myosin Collagen Muscle tissue 100 m Connective tissue 60 m Animation: Structural Proteins Animation: Storage Proteins Animation: Transport Proteins Animation: Receptor Proteins Animation: Contractile Proteins Animation: Defensive Proteins Animation: Hormonal Proteins Animation: Sensory Proteins Animation: Gene Regulatory Proteins 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 Figure 5.UN01 Side chain (R group)  carbon Amino group Carboxyl group Figure 5.16 Nonpolar side chains; hydrophobic Side chain (R group) Glycine (Gly or G) Alanine (Ala or A) Methionine (Met or M) Isoleucine (Ile or I) Leucine (Leu or L) Valine (Val or V) Phenylalanine (Phe or F) Tryptophan (Trp or W) Proline (Pro or P) Polar side chains; hydrophilic Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Electrically charged side chains; hydrophilic Tyrosine (Tyr or Y) Asparagine (Asn or N) Glutamine (Gln or Q) Basic (positively charged) Acidic (negatively charged) Aspartic acid (Asp or D) Glutamic acid (Glu or E) 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, with a carboxyl end (C-terminus) and an amino end (N-terminus) Figure 5.17 Peptide bond New peptide bond forming Side chains Backbone Amino end (N-terminus) Peptide bond Carboxyl end (C-terminus) Protein Structure and Function • A functional protein consists of one or more polypeptides precisely twisted, folded, and coiled into a unique shape Four Levels of Protein Structure • The primary structure of a protein is its unique sequence of amino acids • Secondary structure, found in most proteins, consists of coils and folds in the polypeptide chain • Tertiary structure is determined by interactions among various side chains (R groups) • Quaternary structure results when a protein consists of multiple polypeptide chains Animation: Protein Structure Introduction Figure 5.20a Primary structure Amino acids Amino end Primary structure of transthyretin Carboxyl end • 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 • The coils and folds of secondary structure result from hydrogen bonds between repeating constituents of the polypeptide backbone • Typical secondary structures are a coil called an  helix and a folded structure called a  pleated sheet Animation: Secondary Protein Structure • Tertiary structure is determined by interactions between R groups, rather than interactions between backbone constituents • These interactions between R groups include hydrogen bonds, ionic bonds, hydrophobic interactions, and van der Waals interactions • Strong covalent bonds called disulfide bridges may reinforce the protein’s structure Animation: Tertiary Protein Structure Figure 5.20b Tertiary structure Secondary structure Quaternary structure  helix Hydrogen bond  pleated sheet  strand Hydrogen bond Transthyretin polypeptide Transthyretin protein • Quaternary structure results when two or more polypeptide chains form one macromolecule • Collagen is a fibrous protein consisting of three polypeptides coiled like a rope • Hemoglobin is a globular protein consisting of four polypeptides: two alpha and two beta chains Animation: Quaternary Protein Structure 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 Figure 5.21 Sickle-cell hemoglobin Normal hemoglobin Primary Structure 1 2 3 4 5 6 7 Secondary and Tertiary Structures Quaternary Structure Function Molecules do not associate with one another; each carries oxygen. Normal hemoglobin  subunit  Red Blood Cell Shape  10 m   1 2 3 4 5 6 7 Exposed hydrophobic region Sickle-cell hemoglobin   subunit  Molecules crystallize into a fiber; capacity to carry oxygen is reduced.   10 m 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 Figure 5.22 tu Normal protein Denatured protein Protein Folding in the Cell • It is hard to predict a protein’s structure from its primary structure • Most proteins probably go through several stages on their way to a stable structure • Chaperonins are protein molecules that assist the proper folding of other proteins • Diseases such as Alzheimer’s, Parkinson’s, and mad cow disease are associated with misfolded proteins Figure 5.23 Polypeptide Correctly folded protein Cap Hollow cylinder Chaperonin (fully assembled) Steps of Chaperonin Action: 1 An unfolded polypeptide enters the cylinder from one end. 2 The cap attaches, causing 3 The cap comes the cylinder to change off, and the shape in such a way that properly folded it creates a hydrophilic protein is environment for the released. folding of the polypeptide. Concept 5.5: Nucleic acids store, transmit, and help express 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 made of monomers called nucleotides Figure 5.25-3 DNA 1 Synthesis of mRNA mRNA NUCLEUS CYTOPLASM mRNA 2 Movement of mRNA into cytoplasm Ribosome 3 Synthesis of protein Polypeptide Amino acids The Components of Nucleic Acids • Nucleic acids are polymers called polynucleotides • Each polynucleotide is made of monomers called nucleotides • Each nucleotide consists of a nitrogenous base, a pentose sugar, and one or more phosphate groups • The portion of a nucleotide without the phosphate group is called a nucleoside Figure 5.26 5 end Sugar-phosphate backbone Nitrogenous bases Pyrimidines 5C 3C Nucleoside Nitrogenous base Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA) Purines 5C 1C 5C 3C Phosphate group 3C Sugar (pentose) Guanine (G) Adenine (A) (b) Nucleotide Sugars 3 end (a) Polynucleotide, or nucleic acid Deoxyribose (in DNA) (c) Nucleoside components Ribose (in RNA) • 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 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 The Structures of DNA and RNA Molecules • RNA molecules usually exist as single polypeptide chains • DNA molecules have 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 Figure 5.27 5 3 Sugar-phosphate backbones Hydrogen bonds Base pair joined by hydrogen bonding 3 5 (a) DNA Base pair joined by hydrogen bonding (b) Transfer RNA Figure 5.UN02

The Structure and Function of Large Biological Molecules

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