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