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Unit 4.A 1 – Biomolecules Biomolecules • Biomolecules are molecules that are present in living organisms, including large macromolecules such as proteins, lipids, carbohydrates, and nucleic acids. Biomolecules • **The subcomponents of biological molecules and their sequence determine the properties of that molecule. Biomolecules • A polymer is a large molecule made from repeating subunits called monomers. Biomolecules – The structure and function of polymers are derived from the way their monomers are assembled. Biomolecules • A monomer is a molecule which is able to join with other monomers to make new substances called polymers. Biomolecules • Monomers are assembled into polymers by a condensation reaction, also called a dehydration synthesis reaction. Biomolecules • A dehydration synthesis reaction occurs when two monomers bond together through the loss of a water molecule. Biomolecules • Polymers are disassembled to monomers by hydrolysis, a reaction that is essentially the reverse of the dehydration reaction. Biomolecules • Hydrolysis is a chemical reaction that breaks bonds between two molecules by the addition of water. Biomolecules • The four most important polymers found in living things are: 1. Carbohydrates 2. Lipids 3. Nucleic acids 4. Proteins Biomolecules 1. Carbohydrates are organic compounds that are made up of simple sugars. Biomolecules • **Carbohydrates include sugars and the polymers of sugars. Biomolecules – The monomers of carbohydrates are monosaccharides, or simple sugars. Monosaccharide Biomolecules – Carbohydrate polymers are called polysaccharides. Polysaccharide Biomolecules • **Monosaccharides have molecular formulas that are usually multiples of CH2O. Biomolecules – Glucose (C6H12O6) is the most common monosaccharide. Biomolecules • **Polysaccharides have storage and structural roles; the structure and function of a polysaccharide are determined by its sugar monomers and the positions of glycosidic linkages. Biomolecules • For example: – Starch, a storage polysaccharide of plants, is constructed of monomers of glucose. glucose Starch, made from 1-4 glycosidic linkages Biomolecules • Plants store starch as granules within chloroplasts and other plastids. Biomolecules • For example: – Glycogen, a storage polysaccharide in animals, is made from highly branched chains of glucose. Biomolecules • Animals store starch mainly in liver and muscle cells. Biomolecules • For example: – Cellulose, a major component of plant cell walls; cellulose is a polymer of glucose, and is not digestible by animals. glucose Cellulose, made from 1-4 glycosidic linkages Biomolecules Starch, made from 1-4 glycosidic linkages Cellulose, made from 1-4 glycosidic linkages Biomolecules • For example: – Chitin, a structural polysaccharide, is found in the exoskeleton of arthropods and the cell walls of many fungi. Biomolecules 2. Lipids are nonpolar macromolecules that are insoluble in water and are the one class of large biological molecules that do not form polymers. Biomolecules • **The most biologically important lipids are fats, phospholipids, and steroids. Biomolecules • In general, lipids are nonpolar, having little or no affinity for water. Biomolecules • Lipids are hydrophobic because they consist mostly of hydrocarbons, which form nonpolar covalent bonds. Biomolecules • **Fats are constructed from two types of smaller molecules: glycerol and fatty acids. Biomolecules • Fatty acids are bonded to the glycerol molecule by ester bonds. Biomolecules – The formation of ester linkages is a dehydration synthesis reaction. Biomolecules • **Differences in saturation determine the structure and function of lipids. Biomolecules • Saturated fatty acids have the maximum number of hydrogen atoms possible and no double bonds. Biomolecules • Unsaturated fatty acids have one or more double bonds; this results in a bent structure. Biomolecules • Phospholipids have polar regions that interact with other polar molecules such as water; they also have nonpolar regions that do not interact with water. Biomolecules 3. Nucleic Acids store biological information that is encoded in sequences of monomers called nucleotides. Biomolecules • Each nucleotide has the following structural components: 1. a five-carbon sugar 2. a phosphate group 3. a nitrogen base Biomolecules • Deoxyribose sugar is in DNA and ribose sugar is in RNA. Biomolecules • The bonds that connect nucleotides are called phosphodiester bonds. Biomolecules – Phosphodiester bonds form by condensation reactions. Biomolecules • **DNA and RNA differ in function and differ slightly in structure; these structural differences account for the differing functions. Biomolecules • DNA • Deoxyribose sugar • Thymine • Shape: double helix • RNA • Ribose sugar • Uracil • Shape: single strand Biomolecules 4. Proteins are derived from polypeptides, which are polymers built from the same set of 20 amino acids. Biomolecules • **In proteins, the specific order of amino acid monomers in a polypeptide interacts with the environment to determine the overall shape of the protein. Biomolecules • A functional protein consists of one or more polypeptides twisted, folded, and coiled into a unique shape. Biomolecules • An amino acid contains an amino group, a carboxyl group, and an R group attached to a central carbon. Biomolecules • **Amino acids differ in their properties due to differences in their R groups, also called side chains. Biomolecules • Amino acids are linked by peptide bonds. Biomolecules – Peptide bonds form from condensation, or dehydration synthesis, reactions. Biomolecules • A polypeptide chain is the primary structure of the protein. Biomolecules • The secondary structure of a protein result from hydrogen bonds between amino acids. Biomolecules • Typical secondary structures are a coil called an helix and a folded structure called a pleated sheet. pleated sheet helix Biomolecules • Tertiary structure is determined by interactions between R groups; these interactions include hydrogen bonds, ionic bonds, hydrophobic interactions, and van der Waals interactions. Biomolecules • Strong covalent bonds called disulfide bridges may reinforce the protein’s structure. Biomolecules • Quaternary structure results when two or more polypeptide chains form one macromolecule. Biomolecules • Collagen is a fibrous protein consisting of three polypeptides coiled like a rope. Biomolecules • Hemoglobin is a globular protein consisting of four polypeptides: two alpha and two beta chains. Biomolecules • Denaturation is the loss of a protein’s native structure. Biomolecules • **A denatured protein is biologically inactive. Biomolecules • Proteins are affected by changes in: – pH – Salt concentration – Temperature – Other environmental conditions Biomolecules • Most proteins probably go through several states on their way to a stable structure. Biomolecules • Chaperonins are protein molecules that assist the proper folding of other proteins. Biomolecules • **Directionality influences structure and function of polymers. Biomolecules • For example: – The directionality of DNA determines the direction in which complementary nucleotides are added during DNA synthesis. Biomolecules • For example: – Proteins have an amino end and a carboxyl end. Biomolecules • For example: – The type of bonds between monosaccharides determines their relative orientation in a carbohydrate which determines the secondary structure of the carbohydrate. Homework • Complete handout: – “Biomolecules” • Study for Mini-quiz