AP Biology Chapter 3
Terms
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- Lactase
- Secreted by the digestive cells in the small intestine to absorb sugars from milk.
- Enzyme
- A protein which speeds up a specific chemical reaction.
- Organic compounds
- Carbon-based molecules
- Hydrocarbons
- Composed of only carbon and hydrogen
- Isomer
- Compound with the same molecular formula as another compound, but a different structure. Ex: butane and isobutane
- Functional groups
- The groups of atoms that usually participate in chemical reactions in organic chemistry
- Characteristic of functional groups
- All are polar, which tends to make compounds containing them hydrophilic (water-loving)and souble in water.
- Hydroxyl
- -OH in alcohols
- Carbonyl
-
>C=O
Called a ketone in the middle of a carbon chain, and an aldehyde at the end. - Carboxyl
-
-COOH
Acts as an acid by donating H+ to make carboxylic acids - Amino
-
N<
Make amines. Picks up H+ from solution: base. - Phosphate
- -OPO3 with a -2 charge. Make organic phosphates. Involved in energy transfers
- Macromolecules
- Large biological molecules, include carbs, lipids, proteins, nucleic acids. Can have 1000+ atoms.
- Monomer
- Building blocks of polymers
- Polymer
- Large molecule with many identical or similar molecular units strung together
- Dehydration reaction
- Removes a molecule of H2O and joins two polymers (or monomer and polymer) one donating OH- and one donating H+ to the reaction.
- Hydrolysis
- Opposite of dehydration reaction. Breaks apart polymers by adding H2O to them.
- Monosaccharides
- Carbohydrate monomers. Molecular formulas are a multiple of CH2O.
- Sugar
- A number of hydroxyl groups and a carbonyl group.
- Disaccharides
- Formed by linking two monosaccharides with a dehydration reaction
- Sucrose
- Glucose + fructose
- Maltose
- Glucose and glucose
- Lactose
- Glucose + galactose
- Polysaccharides
- Long chains of sugar units
- Starch
- In roots an dother tissues of plants (only glucose monomers). Serve as sugar stockpiles. Humans use starch by hydrolyzing it in digestive systems.
- Glycogen
- Where animals store excess sugar. More highly branched than starch. Most stores in liver and muscle cells, which hydrolyze the glycogen to use glucose when needed.
- Cellulose
- Most abundant organic compound on Earth. Polymer of glucose. Monomers form an unbranched rod, not coil. Joined by H- bonds.
- Insoluble Fiber
- Cows and termites have cellulose-hydrolyzing microorganisms inside them.
- Lipids
- C and H atoms linked by NONPOLAR covalent bonds. Hydrophobic.
- Fat
- Large lipid mde from glycerol and fatty acids
- Glycerol
- Fatty acid. Main function of fat is energy storage.
- Triglyceride
- 3 fatty acids and 1 glycerol linked by a dehydration reaction.
- Unsaturated
- Less than max hydrogens.
- Saturated
- Only single bonds. Max number of hydrogens.
- Phospholipids
- Like fats, but contain phosphorus and 2 fatty acids.
- Wax
- One fatty acid and an alchohol. More hydrophobic than fats.
- Steroids
- Lipids wth a carbon skeleton bent to form four fused rings. Always 3 six-sided rings and one five sided ring
- Anabolic steroids
- Synthetic variant of testosterone. Use can alter mood, liver function, high blood pressure, infertility, cardiovascular probs.
- Anabolism
- Building of substances by the body
- Proteins
- Polymers consisting of amino acid monomers
- Proteins in the body
- Muscles contain contractile proteins, antibodies, hemoglobin (transport protein for O2), ovalbumin (storage source of amino acids for embryos)
- How are proteins made?
- Proteins are made from amino acids linked by peptide bonds
- Shape of enzymes
- Globular. like lysozyme in tears and white blood cells
- Shape of structural proteins
- in hair and tendons. Long and thing (fibrous)
- High temperatures and proteins
- Can denature proteins (change shape). This is why high fevers can be dangerous.
- Primary protein structure
- Unique sequence of amino acids. Slight change can affect its ability to function
- Secondary protein structure
- Parts of the polypeptide folded or coiled, alpha helix, or pleated sheet.
- Tertiary protein structure
- 3D shape of polypeptide. Globular or fibrous. Restults from interactions among the R groups of the amino acids. May be reinforced further by covalent bonds (disulfide bridges)
- Quaternary protein structure
- Results from the polypeptide chains (subunits). Collagen has 3 pp. chains in a triple helix.
- Linus Pauling
- Found out how hemoglobin carries O2 and how abnormal hemoglobin causes sickle-cell disease. Alpha helix & pleated sheet, also.
- Nucleic acids
- Polymers which are blueprint for proteins
- DNA
- Deoxyribonucleic acid. Double helix shape. A pairs with T, and G with C.
- Interaction btwn. DNA and RNA
- Dna's info is transcribes into RNA, which is translated into primary structure of proteins.
- Genes
- Specific parts of DNA molecule that program amino acid sequences (primary structure)
- Nucleotides
- Monomers in nucleic acids (p.47). 5 carbon sugar (ribose or deoxyribose) + phosphate group + nitrogenous base.
- List the nitrogenous bases found in DNA
-
A- adenine pairs with T- Thymine.
C- Cytosine pairs with G-Guanine. - List the nitrogenous bases found in RNA
- Adenine, Cytosine, Guanine, Uracil (uracil pairs with adenine when it bonds with DNA).
- RNA's shape
- single polynucleotide strand.