Molecules of Life Chapter 3 3.1 Molecules of Life Molecules of life are synthesized by living cells • • • • Carbohydrates Lipids Proteins Nucleic acids Structure to Function Molecules of life differ in three-dimensional structure and function • Carbon backbone • Attached functional groups Structures give clues to how they function Organic Compounds Consist primarily of carbon and hydrogen atoms • Carbon atoms bond covalently with up to four other atoms, often in long chains or rings Functional groups attach to a carbon backbone • Influence organic compound’s properties An Organic Compound: Glucose Four models Functional Groups In alcohols (e.g., sugars, amino acids); water soluble hydroxyl methyl In fatty acid chains; insoluble in water carbonyl (aldehyde) (ketone) In sugars, amino acids, nucleotides; water soluble. An aldehyde if at end of a carbon backbone; a ketone if attached to an interior carbon of backbone carboxyl (non-ionized) (ionized) In amino acids, fatty acids, carbohydrates; water soluble. Highly polar; acts as an acid (releases H+) Fig. 3.3, p. 36 amino In amino acids and certain nucleotide bases; water soluble, acts as a weak base (accepts H+) (non-ionized) (ionized) phosphate icon In nucleotides (e.g., ATP), also in DNA, RNA, many proteins, phospholipids; water soluble, acidic Fig. 3.3, p. 36 Functional Groups: The Importance of Position one of the estrogens testosterone Fig. 3.4, p. 37 Animation: Functional group CLICK HERE TO PLAY Processes of Metabolism Cells use energy to grow and maintain themselves Enzyme-driven reactions build, rearrange, and split organic molecules Building Organic Compounds Cells form complex organic molecules • • • • Simple sugars → carbohydrates Fatty acids → lipids Amino acids → proteins Nucleotides → nucleic acids Condensation combines monomers to form polymers What Cells Do to Organic Compounds Condensation and Hydrolysis enzyme action at functional groups enzyme action at functional groups Condensation Hydrolysis Fig. 3.5, p. 37 Animation: Condensation and hydrolysis CLICK HERE TO PLAY Key Concepts: STRUCTURE DICTATES FUNCTION We define cells partly by their capacity to build complex carbohydrates and lipids, proteins, and nucleic acids The main building blocks are simple sugars, fatty acids, amino acids, and nucleotides These organic compounds have a backbone of carbon atoms with functional groups attached 3.2 Carbohydrates – The Most Abundant Ones Three main types of carbohydrates • Monosaccharides (simple sugars) • Oligosaccharides (short chains) • Polysaccharides (complex carbohydrates) Carbohydrate functions • Instant energy sources • Transportable or storable forms of energy • Structural materials Simple Sugars: Glucose and Fructose Oligosaccharides: Sucrose glucose fructose sucrose c Formation of a sucrose molecule Fig. 3.6, p. 38 Complex Carbohydrates: Bonding Patterns Complex Carbohydrates: Starch, Cellulose, and Glycogen Complex Carbohydrates: Starch, Cellulose, and Glycogen Structure of cellulose c Glycogen. In animals, this polysaccharide is a storage form for excess glucose. It is especially abundant in the liver and muscles of highly active animals, including fishes and people. Fig. 3.8, p. 39 Animation: Structure of starch and cellulose CLICK HERE TO PLAY Complex Carbohydrates: Chitin Key Concepts: CARBOHYDRATES Carbohydrates are the most abundant biological molecules Simple sugars function as transportable forms of energy or as quick energy sources Complex carbohydrates are structural materials or energy reservoirs 3.3 Greasy, Oily – Must Be Lipids Lipids • Fats, phospholipids, waxes, and sterols • Don’t dissolve in water • Dissolve in nonpolar substances (other lipids) Lipid functions • Major sources of energy • Structural materials • Used in cell membranes Fats Lipids with one, two, or three fatty acid tails • Saturated • Unsaturated (cis and trans) Triglycerides (neutral fats ) • Three fatty acid tails • Most abundant animal fat (body fat) • Major energy reserves Fatty Acids Animation: Fatty acids CLICK HERE TO PLAY Trans and Cis Fatty Acids Triglyceride Formation glycerol three fatty acid tails Triglyceride, a neutral fat Fig. 3.11, p. 40 Animation: Triglyceride formation CLICK HERE TO PLAY Phospholipids Main component of cell membranes • Hydrophilic head, hydrophobic tails hydrophilic head two hydrophilic tails b Fig. 3.13, p. 41 c Cell membrane section Fig. 3.13, p. 41 Animation: Phospholipid structure CLICK HERE TO PLAY Waxes Firm, pliable, water repelling, lubricating Sterols: Cholesterol Membrane components; precursors of other molecules (steroid hormones) Animation: Cholesterol CLICK HERE TO PLAY Key Concepts: LIPIDS Complex lipids function as energy reservoirs, structural materials of cell membranes, signaling molecules, and waterproofing or lubricating substances 3.4 Proteins – Diversity in Structure and Function Proteins have many functions • • • • • • Structures Nutrition Enzymes Transportation Communication Defense Protein Structure Built from 20 kinds of amino acids Fig. 3.15, p. 42 amino group carboxyl group Fig. 3.15, p. 42 Fig. 3.15, p. 42 valine Fig. 3.15, p. 42 Protein Synthesis Protein Synthesis Protein Synthesis Four Levels of Protein Structure 1. Primary structure • Amino acids joined by peptide bonds form a linear polypeptide chain 2. Secondary structure • Polypeptide chains form sheets and coils 3. Tertiary structure • Sheets and coils pack into functional domains Four Levels of Protein Structure 4. Quaternary structure • Many proteins (e.g. enzymes) consist of two or more chains Other protein structures • Glycoproteins • Lipoproteins • Fibrous proteins Levels of Protein Structure a Protein primary structure: Amino acids bonded in a polypeptide chain. Fig. 3.17, p. 43 Levels of Protein Structure b Protein secondary structure: A coiled (helical) or sheetlike array, held in place by hydrogen bonds ( dotted lines) between different parts of the polypeptide chain. helical coil sheet Fig. 3.17, p. 43 Levels of Protein Structure barrel c Protein tertiary structure: A chain’s coiled parts, sheetlike arrays, or both have folded and twisted into stable, functional domains, including clusters, pockets, and barrels. Fig. 3.17, p. 43 Levels of Protein Structure d Protein quaternary structure: Many weak interactions hold two or more polypeptide chains together as a single molecule. Fig. 3.17, p. 43 Animation: Structure of an amino acid CLICK HERE TO PLAY Animation: Peptide bond formation CLICK HERE TO PLAY Animation: Secondary and tertiary structure CLICK HERE TO PLAY Animation: Globin and hemoglobin structure CLICK HERE TO PLAY 3.5 Why is Protein Structure So Important? Protein structure dictates function Sometimes a mutation in DNA results in an amino acid substitution that alters a protein’s structure and compromises its function • Example: Hemoglobin and sickle-cell anemia Normal Hemoglobin Structure alpha globin heme a Globin. The secondary structure of this polypeptide includes several helixes. The coils fold up to form a pocket that cradles heme, a functional group with an iron atom at its center. The kind of molecular representation shown here is called a ribbon model, after its appearance. Appendix V has more details about such models. Fig. 3.18, p. 44 Normal Hemoglobin Structure alpha globin beta globin alpha globin beta globin b Hemoglobin is one of the proteins with quaternary structure. It consists of four globin molecules held together by hydrogen bonds. To help you distinguish among them, the two alpha globin chains are shown here in green, and the two beta globins are in brown. Fig. 3.18, p. 44 Sickle-Cell Mutation VALINE HISTIDINE LEUCINE THREONINE PROLINE GLUTAMATE GLUTAMATE a Normal amino acid sequence at the start of a beta chain for hemoglobin. Fig. 3.19, p. 45 Sickle-Cell Mutation VALINE HISTIDINE LEUCINE THREONINE PROLINE b One amino acid substitution results in the abnormal beta chain in HbS molecules. Instead of glutamate, valine was added at the sixth position of the polypeptide chain. c Glutamate has an overall negative charge; valine has no net charge. At low oxygen levels, this difference gives rise to a water-repellent, sticky patch on HbS molecules. They stick together because of that patch, forming rodshaped clumps that distort normally rounded red blood cells into sickle shapes. (A sickle is a farm tool that has a crescent-shaped blade.) VALINE GLUTAMATE sickle cell normal cell Fig. 3.19, p. 45 Sickle-Cell Mutation Clumping of cells in bloodstream Circulatory problems, damage to brain, lungs, heart, skeletal muscles, gut, and kidneys Heart failure, paralysis, pneumonia, rheumatism, gut pain, kidney failure Spleen concentrates sickle cells Spleen enlargement Immune system compromised Rapid destruction of sickle cells d Melba Moore, celebrity spokesperson for sickle-cell anemia organizations. Right, range of symptoms for a person with two mutated genes for hemoglobin’s beta chain. Anemia, causing weakness,fatigue, impaired development,heart chamber dilation Impaired brain function, heart failure Fig. 3.19, p. 45 Clumping of cells in bloodstream Circulatory problems, damage to brain, lungs, heart, skeletal muscles, gut, and kidneys Heart failure, paralysis, pneumonia, rheumatism, gut pain, kidney failure Spleen concentrates sickle cells Spleen enlargement Immune system compromised Rapid destruction of sickle cells d Melba Moore, celebrity spokesperson for sickle-cell anemia organizations. Right, range of symptoms for a person with two mutated genes for hemoglobin’s beta chain. Anemia, causing weakness,fatigue, impaired development,heart chamber dilation Stepped Art Impaired brain function, heart failure Fig. 3-19, p. 45 Animation: Sickle-cell anemia CLICK HERE TO PLAY Denatured Proteins If a protein unfolds and loses its threedimensional shape (denatures), it also loses its function Caused by shifts in pH or temperature, or exposure to detergent or salts • Disrupts hydrogen bonds and other molecular interactions responsible for protein’s shape Key Concepts: PROTEINS Structurally and functionally, proteins are the most diverse molecules of life They include enzymes, structural materials, signaling molecules, and transporters Animation: Molecular models of the protein hemoglobin CLICK HERE TO PLAY 3.6 Nucleotides, DNA, and RNAs Nucleotide structure, 3 parts: • Sugar • Phosphate group • Nitrogen-containing base base (blue) sugar (orange) three phosphate groups Fig. 3.20, p. 46 Nucleotide Functions: Reproduction, Metabolism, and Survival DNA and RNAs are nucleic acids, each composed of four kinds of nucleotide subunits ATP energizes many kinds of molecules by phosphate-group transfers Other nucleotides function as coenzymes or as chemical messengers Nucleotides of DNA phosphate group sugar (deoxyribose) adenine (A) base with a double-ring structure Fig. 3.21, p. 46 THYMINE (T) base with a single-ring structure Fig. 3.21, p. 46 GUANINE (C) base with a double-ring structure Fig. 3.21, p. 46 CYTOSINE (C) base with a single-ring structure Fig. 3.21, p. 46 DNA, RNAs, and Protein Synthesis DNA (double-stranded) • Encodes information about the primary structure of all cell proteins in its nucleotide sequence RNA molecules (usually single stranded) • Different kinds interact with DNA and one another during protein synthesis The DNA Double-Helix covalent bonding in carbon backbone hydrogen bonding between bases Fig. 3.22, p. 47 Key Concepts: NUCLEOTIDES AND NUCLEIC ACIDS Nucleotides have major metabolic roles and are building blocks of nucleic acids Two kinds of nucleic acids, DNA and RNA, interact as the cell’s system of storing, retrieving, and translating information about building proteins Animation: Nucleotide subunits of DNA CLICK HERE TO PLAY Animation: Structure of ATP CLICK HERE TO PLAY