Bài giảng The molecules of cells
Got Lactose?
Lactose intolerance illustrates the importance of biological molecules to the functioning of living cells and to human health
Molecular interactions, such as those between the gene for lactase production, the enzyme lactase, and the milk sugar lactose, drive all biological processes
Life's molecular diversity is based on the properties of carbon
Organic compounds contain at least one carbon atom
Covalent bonding enables carbon to form complex structures
A carbon atom has four electrons in its outer shell
To complete the shell, it can form four covalent bonds
The way bonding occurs among atoms determines the overall shape of the molecule
g model Methane The 4 single bonds of carbon point to the corners of a tetrahedron. LE 3-1b Ethane Propane Carbon skeletons vary in length. LE 3-1c Butane Isobutane Skeletons may be unbranched or branched. LE 3-1d 1- Butene 2- Butene Skeletons may have double bonds, which can vary in location. LE 3-1e Skeletons may be arranged in rings. Cyclohexane Benzene Animation: Carbon Skeletons Animation: Isomers Animation: L-Dopa Hydrocarbons are composed of only hydrogen and carbon A series of covalently bonded carbons forms the carbon skeleton of the molecule Isomers are molecules with the same molecular formula but different structures and properties 3.2 Functional groups help determine the properties of organic compounds Functional groups are groups of atoms attached to the carbon skeleton of molecules Usually participate in chemical reactions Give organic molecules their particular properties LE 3-2 Estradiol Female lion Male lion Testosterone Five main functional groups are important in the chemistry of life: Hydroxyl group Carbonyl group Carboxyl group Amino group Phosphate group These groups are all polar and make compounds containing them hydrophilic (water-loving) 3.3 Cells make a huge number of large molecules from a small set of small molecules Four main classes of biological macromolecules Carbohydrates Lipids Proteins Nucleic acids Cells make the most of their large molecules by joining smaller organic monomers into chains called polymers Monomers are usually linked by dehydration reactions A water molecule is removed Animation: Polymers LE 3-3a Short polymer Unlinked monomer Dehydration reaction Longer polymer Polymers are broken down to monomers by the reverse process, hydrolysis A water molecule is added LE 3-3b Hydrolysis CARBOHYDRATES 3.4 Monosaccharides are the simplest carbohydrates Monosaccharides (single sugars) are carbohydrate monomers A monosaccharide has a formula that is a multiple of CH2O Contains hydroxyl groups and a carbonyl group May be isomers, such as glucose and fructose May take chain or ring forms LE 3-4b Glucose Fructose LE 3-4c Structural formula Abbreviated structure Simplified structure 3.5 Cells link two single sugars to form disaccharides Two monosaccharides can join to form a disaccharide Linked by a dehydration reaction Example: two glucose monomers form the disaccharide maltose Animation: Disaccharides LE 3-5 Glucose Glucose Maltose CONNECTION 3.6 How sweet is sweet? We perceive a sweet taste when a chemical binds to the sweet receptor on the tongue The structure of a compound determines how well it fits into a receptor The more strongly the chemical binds to the receptor, the sweeter it is perceived to be The chemical can be sugar or another compound, such as aspartame 3.7 Polysaccharides are long chains of sugar units Polysaccharides are polymers of monosaccharides linked together by dehydration reactions Some polysaccharides are storage molecules Starch in plants Glycogen in animals Some polysaccharides serve as structural compounds Cellulose in plants Animation: Polysaccharides LE 3-7 Starch granules in potato tuber cells Glycogen granules in muscle tissues Cellulose fibrils in a plant cell wall Cellulose molecules G LYCOGEN C ELLULOSE S TARCH Glucose monomer LIPIDS 3.8 Fats are lipids that are mostly energy-storage molecules Lipids are diverse compounds consisting mainly of carbon and hydrogen atoms Linked by nonpolar covalent bonds Hydrophobic (water-fearing) Animation: Fats Fats, also called triglycerides, are lipids whose main function is energy storage Polymers of fatty acids (usually three molecules) and one glycerol molecule Formed by dehydration reactions Saturated fatty acids Contain the maximum number of hydrogens Have no double bonds between carbons Unsaturated fatty acids Contain fewer than the maximum possible hydrogens Have double bonds between carbons Oils are liquid fats 3.9 Phospholipids, waxes, and steroids are lipids with a variety of functions Phospholipids Contain two fatty acid groups and the element phosphorus Are a major component of cell membranes Waxes Consist of a single fatty acid linked to an alcohol Form waterproof coatings Steroids Have backbones bent into rings, as in cholesterol Are often hormones or the basis of hormones CONNECTION 3.10 Anabolic steroids pose health risks Anabolic steroids are natural and synthetic variants of the male hormone testosterone Build up bone and muscle mass Can cause serious health problems PROTEINS 3.11 Proteins are essential to the structures and activities of life A protein is a polymer constructed from amino acid monomers The structure of the protein determines its function The seven major classes of protein are Structural: hair, cell cytoskeleton Contractile: producers of movement in muscle and other cells Storage: sources of amino acids, such as egg white Defense: antibodies, membrane proteins Transport: carriers of molecules such as hemoglobin, membrane proteins Signaling: hormones, membrane proteins Enzymes: regulators of the speed biochemical reactions Animation: Structural Proteins Animation: Storage Proteins Animation: Transport Proteins Animation: Receptor Proteins Animation: Contractile Proteins Animation: Defensive Proteins Animation: Enzymes Animation: Hormonal Proteins Animation: Sensory Proteins Animation: Gene Regulatory Proteins 3.12 Proteins are made from amino acids linked by peptide bonds Protein diversity is based on different arrangements of a common set of 20 amino acid monomers Each amino acid contains An amino group A carboxyl group One of twenty functional ("R") groups The three groups and a hydrogen atom are bonded to a central "alpha" carbon LE 3-12a Carboxyl (acid) group Amino group The structure of the R group determines the specific properties of each amino acid An amino acid may be hydrophobic or hydrophilic, depending on the characteristics of the R group LE 3-12b Leucine ( Leu ) Serine (Ser) Hydrophobic Hydrophilic Aspartic acid (Asp) Cells link amino acids together by dehydration synthesis The bonds between amino acid monomers are called peptide bonds Dipeptides are two amino acids long; polypeptides are from several to more than a thousand amino acids long LE 3-12c Amino acid Dipeptide Amino acid Peptide bond Dehydration reaction Amino group Carboxyl group 3.13 A protein's specific shape determines its function A protein consists of one or more polypeptide chains spontaneously folded into a unique shape LE 3-13 Groove Groove The folding of a polypeptide creates grooves that enable other molecules to bind to it In denaturation , chemical or physical changes can cause proteins to lose their shape and thus their specific function 3.14 A protein's shape depends on four levels of structure Primary structure: the unique sequence of amino acids forming the polypeptide Secondary structure: the coiling or folding of the chain, stabilized by hydrogen bonding May be alpha helix or pleated sheet (which dominates the silk protein of a spider's web) Tertiary structure: the overall three-dimensional shape of the polypeptide Quaternary structure: the association of two or more polypeptide chains (subunits) LE 3-14a Levels of Protein Structure Amino acids LE 3-14b Levels of Protein Structure Amino acids Hydrogen bond Alpha helix Pleated sheet LE 3-14c Levels of Protein Structure Amino acids Hydrogen bond Alpha helix Pleated sheet Polypeptide (single subunit of transthyretin ) LE 3-14d Levels of Protein Structure Amino acids Hydrogen bond Alpha helix Pleated sheet Polypeptide (single subunit of transthyretin ) Transthyretin , with four identical polypeptide subunits Animation: Protein Structure Introduction Animation: Primary Protein Structure Animation: Secondary Protein Structure Animation: Tertiary Protein Structure Animation: Quarternary Protein Structure Collagen is an example of a protein with a quaternary structure Three subunits wound into a helix Structure provides great strength to long fibers TALKING ABOUT SCIENCE 3.15 Linus Pauling contributed to our understanding of the chemistry of life Felt that the study of individual parts must come first, then putting the parts together Began his career by studying chemical bonding First described the alpha helix and pleated sheet protein structures Discovered how abnormal hemoglobin causes sickle cell disease Won two Nobel prizes, for chemistry and for peace (for helping produce a nuclear test ban treaty) NUCLEIC ACIDS 3.16 Nucleic acids are information-rich polymers of nucleotides There are two types of nucleic acid-DNA and RNA Nucleic acids are polymers of nucleotide monomers composed of A five-carbon sugar A phosphate group A nitrogenous base-adenine (A), thymine (T), cytosine ( C), and guanine (G) in DNA; A, G, C, and uracil (U) in RNA LE 3-16a Nitrogenous base (A) Sugar Phosphate group Nucleotide monomers are formed into a polynucleotide with a sugar-phosphate backbone and attached nitrogenous bases LE 3-16b Nucleotide Sugar-phosphate backbone Hydrogen bonding between nitrogenous bases creates the final structure of the nucleic acid RNA usually consists of a single polynucleotide strand DNA is a double helix Two polynucleotides are twisted around each other Nitrogenous bases protruding from the backbone pair with each other, A with T and G with C LE 3-16c Base pair Specific sequences of DNA make up genes that program the amino acid sequences of proteins
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