Lecture Outline
Carbon, Carbon in the Sky--Are You Swinging Low and High?
- Coniferous trees are the premier producers of the great northern forests.
- They take in large amounts of carbon dioxide during photosynthesis.
- Carbon dioxide levels in the atmosphere decline during the warm months.
- An indication that the earth may be getting warmer, earlier is the shift toward breaking dormancy earlier in the growing season.
- Carbon in its many forms permeates the entire world of life.
3.1 The Molecules of Life--From Structure to Function
- What Is An Organic Compound?
- Only living cells can synthesize carbohydrates, lipids, proteins, and nucleic acids.
- These molecules are organic compounds consisting of carbon and one or more additional elements, covalently bonded to one another.
- It All Starts With Carbon's Bonding Behavior
- Oxygen, hydrogen, and carbon are the most abundant elements in living matter.
- Much of the H and O are linked as water.
- Carbon can share pairs of electrons with as many as four other atoms to form organic molecules of several configurations.
- Ways of Representing Organic Compounds
- A ball-and-stick model depicts bonding of atoms; space-filling models convey a molecule's size and surfaces.
- Larger molecules are best visualized using ribbon models, such as those generated by computer programs.
3.2 Overview of Functional Groups
- Functional groups are atoms or groups of atoms covalently bonded to a carbon backbone; they convey distinct properties, such as solubility and chemical reactivity, to the complete molecule.
- The common functional groups in biological molecules are: hydroxyl, methyl, carbonyl, carboxyl, amino, phosphate, and sulfhydryl.
3.3 How Do Cells Build Organic Compounds?
- Four Families of Building Blocks
- Simple sugars, fatty acids, amino acids, and nucleotides are the four major families of small building blocks.
- Monomers can be joined to form larger polymers.
- Five Categories of Reactions
- Enzymes are a special class of proteins that mediate five categories of reactions:
- functional-group transfer from one molecule to another,
- electron transfer --stripped from one molecule and given to another,
- rearrangement of internal bonds converts one type of organic molecule to another,
- condensation of two molecules into one,
- cleavage of one molecule into two.
- In a condensation reaction, one molecule is stripped of its H+, another is stripped of its OH-; then the two molecule fragments join to form a new compound and the H+ and OH- form water.
- Hydrolysis is the reverse: one molecule is split by the addition of H+ and OH- (from water) to the components.
3.4 Carbohydrates--The Most Abundant Molecules of Life
- The Simple Sugars
- Monosaccharides--one sugar unit--are the simplest carbohydrates.
- They are characterized by solubility in water, sweet taste, and several -OH groups.
- Ribose and deoxyribose (five-carbon backbones) are building blocks for nucleic acids.
- Glucose and fructose (six-carbon backbones) are used in assembling larger carbohydrates.
- Other important molecules derived from sugar monomers include glycerol and vitamin C.
- Short-Chain Carbohydrates
- An oligosaccharide is a short chain of two or more sugar monomers.
- Disaccharides--two sugar units--are the simplest.
- Lactose (glucose + galactose) is present in milk.
- Sucrose (glucose + fructose) is a transport form of sugar used by plants and harvested by humans for use in food.
- Maltose (two glucose units) is present in germinating seeds.
- Oligosaccharides with three or more sugar monomers are attached as short side chains to proteins where they participate in membrane function.
- Complex Carbohydrates
- A polysaccharide is a straight or branched chain of hundreds or thousands of sugar monomers.
- Starch is a plant storage form of energy, arranged as unbranched coiled chains, easily hydrolyzed to glucose units.
- Cellulose is a fiberlike structural material--tough, insoluble--used in plant cell walls.
- Glycogen is a highly-branched chain used by animals to store energy in muscles and liver.
- Chitin is a specialized polysaccharide with nitrogen attached to the glucose units; it is used as a structural material in arthropod exoskeletons and fungal cell walls.
3.5 Greasy, Oily--Must Be Lipids
- Lipids are greasy or oily compounds with little tendency to dissolve in water.
- They can be broken down by hydrolysis reactions.
- They function in energy storage, membrane structure, and coatings.
- Fats and Fatty Acids
- A fatty acid is a long chain of mostly carbon and hydrogen atoms with a -COOH group at one end.
- When they are part of complex lipids, the fatty acids resemble long, flexible tails.
- Unsaturated fats are liquids (oils) at room temperature because one or more double bonds between the carbons in the fatty acids permits "kinks" in the tails.
- Saturated fats (triglycerides) have only single C--C bonds in their fatty acid tails and are solids at room temperature.
- Fats are formed by the attachment of one (mono-), two (di-), or three (tri-) fatty acids to a glycerol.
- They are a rich source of energy, yielding more than twice the energy per weight basis as carbohydrates.
- They are also provide an insulation blanket for animals that must endure cold, harsh temperatures.
- Phospholipids
- These are formed by attachment of two fatty acids plus a phosphate group to a glycerol.
- They are the main structural material of membranes where they arrange in bilayers.
- Sterols and Their Derivatives
- Sterols have a backbone of four carbon rings but no fatty acid tails.
- Cholesterol is a component of cell membranes in animals and can be modified to form sex hormones (testosterone and estrogen) and vitamin D.
- Waxes
- They are formed by attachment of long-chain fatty acids to long-chain alcohols or carbon rings.
- They serve as coatings for plant parts and as animal coverings.
3.6 A String of Amino Acids: Protein Primary Structure
- Proteins function as enzymes, in cell movements, as storage and transport agents, as hormones, as antibodies, and as structural material.
- Amino Acid Structure
- Amino acids are small organic molecules with an amino group, a carboxyl group, and one of twenty varying R groups.
- All of the parts of an amino acid molecule are covalently bonded to a central carbon atom.
- Polypeptide Chain Formation
- Primary structure is defined as ordered sequences of amino acids each linked together by peptide bonds to form polypeptide chains.
- There are 20 kinds of amino acids available in nature.
- The sequence of the amino acids is determined by DNA and is unique for each kind of protein.
- Fibrous proteins have polypeptide chains organized as strands or sheets; they contribute to the shape, internal organization, and movement of cells.
- Globular proteins, including most enzymes, have their chains folded into compact, rounded shapes.
3.7 How Does a Protein's Final Structure Emerge?
- Second and Third Levels of Protein Structure
- Secondary structure refers to the helical coil (as in hemoglobin) or sheetlike array (as in silk) that results from hydrogen bonding of side groups on the amino acid chains.
- Tertiary structure is the result of folding due to interactions among R groups along the polypeptide chain.
- Fourth Level of Protein Structure
- Quaternary structure describes the complexing of two of more polypeptide chains.
- Hemoglobin is a good example of four interacting chains that form a globular proteins; keratin and collagen are complex fibrous proteins.
- Glycoproteins consist of oligosaccharides covalently bonded to proteins; they are abundant on the exterior of animal cells, as cell products, and in the blood.
- Lipoproteins have both lipid and protein components; they transport fats and cholesterol in the blood.
- Denaturation--How to Undo the Structure
- High temperatures or changes in pH can cause a loss of a protein's normal three-dimensional shape (denaturation).
- Normal functioning is lost upon denaturation, which is often irreversible (for example, a cooked egg).
3.8 Why Is Protein Structure So Important?
- Just One Wrong Amino Acid...
- Alteration of a cell's DNA can result in the wrong amino acid insertion in a polypeptide chain.
- If valine is substituted for glutamate in hemoglobin, the result is called HbS.
- Sickle-Shaped Cells and a Serious Disorder
- Persons who inherit two mutated genes for the beta chain of hemoglobin can only make HbS.
- The altered hemoglobin causes the red blood cells to be misshapen--sickle-cell anemia, with many serious body dysfunctions.
3.9 Nucleotides and Nucleic Acids
- The Diverse Roles of Nucleotides
- Each nucleotide consists of a five-carbon sugar (ribose or deoxyribose), a nitrogen-containing base, and a phosphate group.
- Adenosine phosphates are chemical messengers (cAMP) or energy carriers (ATP).
- Nucleotide coenzymes transport hydrogen atoms and electrons (examples: NAD+ and FAD).
- Nucleotides also serve as building blocks for nucleic acids.
- Regarding DNA and the RNAs
- Nucleic acids are polymers of nucleotides.
- Four different kinds of nucleotides are strung together to form large single or double-stranded molecules.
- Each strand's backbone consists of joined sugars and phosphates with nucleotide bases projecting toward the interior.
- The two most important nucleic acids are DNA and RNA.
- DNA is a double-stranded helix carrying encoded hereditary instructions.
- RNA is single stranded and functions in translating the code to build proteins.
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