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32 Cards in this Set
- Front
- Back
Monomers of nucleic acids
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Nucleotides (be able to draw one)
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Monomers of proteins
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Amino acids (be able to draw one)
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Structure of carbohydrates
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1:2:1 ratio between carbon, hydrogen, and oxygen
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Most common elements in living things
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carbon (C), hydrogen (H), oxygen (O), nitrogen (N)
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Elements important to living things
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sulfur (S), calcium (Ca), phosphorus (P), iron (Fe), sodium (Na)
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Properties of water
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Polar, cohesive, has high specific heat, and is an excellent solvent.
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Organic Molecules
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Contain carbon and hydrogen and are found in living organisms.
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monosaccharides
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glucose, galactose, fructose
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disaccharides
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maltose, lactose, and sucrose
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disaccharides
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maltose, lactose, and sucrose
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polysaccharides
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starch, glycogen, and cellulose
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Draw me!
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amino acid
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Draw me!
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glucose
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Draw me!
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fatty acid
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Draw me!
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nucleotide
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condensation reaction
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two monomers react to form a dimer, water is a product.
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hydrolysis reaction
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one dimer (or polymer) becomes two monomers, water is a product.
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functions of lipids
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energy storage, thermal insulation, protection of internal organs, major component of cell membranes.
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function of amino acids
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create proteins
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functions of carbohydrates
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energy and structural support
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functions of nucleotides
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passage of genetic information from parent to offspring, creation of proteins.
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function of proteins
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structural support, transport, movement, defence, metabolism
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globular proteins
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water soluble, have round (globby) shape.
Enzymes are typically globular proteins |
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fibrous proteins
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water insoluble, long, stringy shape.
Collagen is an example of a fibrous protein |
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enzymes
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proteins that catalyze chemical reactions.
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allosteric inhibition
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enzyme inhibition caused by binding to a site other than the active site
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competitive inhibition
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enzyme inhibition caused by binding of an inhibitor to the active site, blocking the substrate
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coenzyme
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a molecule (often a vitamin) that increases enzyme activity by binding to an allosteric site.
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Primary Protein Structure
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Order of amino acids. Peptide bonds hold amino acids together.
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Secondary Protein Structure
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Repeated "motifs" or patterns in the polypeptide that form either a helix or a pleated sheet. Stabilized by hydrogen bonds.
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Tertiary Protein Structure
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Interactions between the variable "R" groups that cause the polypeptide's "nascent" folded form. Bonds can be ionic, covalent, hydrogen, or disulfide.
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Quaternary Protein Structure
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Interactions between several polypeptides to form the completed and functioning protein.
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