Biochemistry

Cards (115)

  • cAMP
    used in hormone interactions
  • NAD+ and FAD
    Used to produce ATP.
  • ATP
    -primary energy currency of cell
    -generated during glucose catabolism
    -energy stored in high-energy phosphate bonds
  • Nucleotides
    Important in cell energy transformations
  • complementary base pairing
    In DNA, T pairs with A; G pairs with C;
    RNA, U pairs with A and G pairs with C
  • Antiparallel
    The opposite arrangement of the sugar-phosphate backbones in a DNA double helix.
  • Antiparallel
    One DNA strand terminates with a 5' carbon end and 3' carbon end. One strand is said to run 5' to 3'; the opposite DNA strand runs antiparallel, or 3' to 5'.

    RNA remains single, DNA becomes a double strand.
  • phosphodiester bond

    Nucleotides attached by this bond.
  • Purines
    Two-Ringed
  • Pyrimidines
    Single ringed
  • Nucletotides are made of?
    Pentose sugar (ribose - RNA and deoxyribose - DNA)

    Phosphate group

    Nitrogenous base (AGCT for DNA and AGCU for RNA).
  • RNA
    Involved in protein synthesis and hereditary information for some viruses, remaining single-stranded.
  • DNA
    Stores hereditary information and is composed of two strands held together by hydrogen bonds between complementary nitrogenous bases.
  • Nucleic Acids
    Serve as assembly instructions for all proteins in living organisms, consisting of DNA and RNA.

    It's also the polymers of nucleotides.
  • Peptide Bonds
    Bonds formed by a condensation/dehydration reaction between the amino group of one amino acid and the carboxyl group of the adjacent amino acid.
  • The 8 Essential Amino Acids
    Valine, Leucine, Isoleucine, Methionine, Phenylalanine, Tryptophan, Threonine and Lysine
  • Amino Acids
    The building blocks of proteins, consisting of a central carbon atom with an attached amino group, carboxyl group, hydrogen atom, and a variable side chain.
  • Quarternary Protein Structure
    Formed when two or more polypeptide subunits come together to form a functional protein.
    The same bonds and forces that hold the tertiary structure together can stabilize the quaternary structure.
  • Disulfide Bridge
    When two cysteine residues are close together, their sulfur atoms can form a covalent bond.
  • Tertiary Protein Structure
    Structure formed due to bonding interactions among the amino acid R groups.
    Amino acids with polar R groups are attracted to water, while those with nonpolar R groups are excluded (therefore, they tend to congregate to the interior of the folded polypeptide).

    It's stabilized by interactions of R groups:

    Hydrogen bonds between certain polar side chains Ionic bonds between oppositely charged side chains, and Van der Waals forces between non-polar R groups

    The amino acid proline forms a natural kink wherever it occurs
  • Beta Pleated Sheet
    forms when two parts of the polypeptide chain lie parallel to one another and H bonds form between the two strands.
  • Alpha Helix
    Coils and folds in a polypeptide caused by hydrogen bonds between the oxygen (carboxyl group) of one peptide bond and hydrogen (amino group) found four peptide bonds away
  • Secondary Protein Structure
    Regions where the polypeptide is folded into localized shapes.

    It has two types: alpha helix and beta-pleated sheet.
  • Primary Protein Structure
    Unique sequence of amino acids in a polypeptide chain

    Determined by the nucleotide sequence in a gene in DNA
  • Proteins
    Used as a structural building block and functional molecules in cells, formed by a specific sequence of amino acids.
  • Waxes
    Long-chain fatty acids linked to alcohols or carbon rings, forming hydrophobic, soft solids used.
    Form waterproof coating on various animals and plants.
  • Steroids
    Hydrophobic molecules containing 4 fused hydrocarbon rings with different functional groups attached.
  • Phospholipids
    Major component of cell membranes, composed of glycerol, two fatty acids, and a phosphate group.

    The highly polar phosphate group forms the polar head (hydrophilic) and fatty acids from long nonpolar tails (hydrophobic).
  • Unsaturated Fats
    Contain Unsaturated fatty acids.
  • Saturated Fats
    Contain Saturated fatty acids.

    Tend to be solid at room temp.
  • Adipose
    Layer of fatty tissue under skin as insulation in mammals and birds.
  • What process occurs to form fats? What's the resulting bond?
    Esterification, Ester Linkage
  • How are fats formed?
    Formed by a condensation reaction between the hydroxyl group of the glycerol and the carboxyl group on the fatty acid
  • Trigylceride
    Most common fat.

    Composed of three fatty acid chains linked to a glycerol molecule
  • Fats
    Lipids made of fatty acid and glycerol molecules, functioning as stored energy and insulation.

    Functions as stored energy - double the energy of carbohydrates.
  • Unsaturated Fatty Acids
    Fatty acids with one or more double bonds between carbon atoms.
  • Saturated Fatty Acids
    Fatty acids with only single bonds between carbon atoms.
  • Fatty Acids
    The structural backbone of most lipids, consisting of a hydrocarbon chain with a carboxyl group at one end.

    As its length increases, its solubility decreases.
  • Lipids
    hydrophobic molecules composed of hydrogen, carbon, and lesser amounts of oxygen, used to store energy, build membranes, and other cell parts as chemical signaling molecules.
  • Chitin
    Hard exoskeleton of insects and crustaceans and the cell walls of many fungi.

    2nd most abundant organic material in nature.

    Cellulose-like polymer of N-acetylglucosamine (monomer is glucose is with a nitrogen-containing group on the second carbon)