AP Biology Chapter 1 Test Guide with
Questions Solved 100% Correct
steroids - ✔-structure: carbon skeleton of four fused rings with different chemicals
attached -with a different functional group attached you create a new one -ex: cholesterol
and sex hormones
cholesterol - ✔-important cell component
-animal cell membranes
-helps keep membrane fluid, flexible and
mobile -precursor of all other steroids
~including vertebrate sex hormones
-high levels in blood may contribute to cardiovascular disease
proteins - ✔-most structurally and functionally diverse
group -function: involved in almost everything ~enzymes
(pepsin, DNA polymerase)
~structure (keratin, collagen)
~carriers and transport (hemoglobin, aquaporin)
~cell communication (signals and receptors)
~defense (antibodies)
~movement (actin and myosin)
~storage (bean seed)
-structure:
~monomer amino acids
~polymer polypeptide
-can be one or more polypeptide chains folded and bonded together
,-large and complex molecules
-complex 3D shape
amino acids - ✔-structure: central carbon (alpha carbon)
-amino group
-carboxyl group (acid)
-R group (side chain)
~variable group
~different for each
~confers unique chemical properties
-physical and chemical properties based on R groups attached
peptide bonds - ✔-covalent bond between NH2 (amine) of one amino acid and
COOH (carboxyl) of another
-C-N bond
protein structure - ✔-a polypeptide chain that has been folded, twisted and coiled into
unique shapes
-performed as soon as the polypeptide is formed by creating bonds between parts of the chain
-the specific structure determines the function
primary structure - ✔-unique sequence of amino
acids -amino acid sequence determined by gene (DNA)
-slight change in amino acid sequence can affect protein's structure and its function
, secondary structure - ✔-localized folding or pleating of parts of the protein
chain -result of H bonds between repeating structures of polypeptide -weak
bonds
-α helix and β pleated sheets
tertiary structure - ✔-whole molecule folding
-interactions between distant amino acids
-hydrophobic interactions
~cytoplasm is water-based
~nonpolar amino acids cluster away from water
-H bonds and ionic bonds
-disulfide bridges
~covalent bonds between sulfurs in sulfhydryls (S-H)
~anchors 3D shape
quaternary structure - ✔-more than one polypeptide chain bonded
together -only then does polypeptide become functional protein -
hydrophobic interactions
denaturation - ✔-although proteins fold as they are made, under certain conditions,
these proteins will not fold properly
-can be caused by heat, change in pH, change in solution, or salinity
-will be inactive
-some proteins will be able to regain their original structure by removing the elements
nucleic acid - ✔-function: genetic material
-stores information; genes, blueprint for building proteins
Questions Solved 100% Correct
steroids - ✔-structure: carbon skeleton of four fused rings with different chemicals
attached -with a different functional group attached you create a new one -ex: cholesterol
and sex hormones
cholesterol - ✔-important cell component
-animal cell membranes
-helps keep membrane fluid, flexible and
mobile -precursor of all other steroids
~including vertebrate sex hormones
-high levels in blood may contribute to cardiovascular disease
proteins - ✔-most structurally and functionally diverse
group -function: involved in almost everything ~enzymes
(pepsin, DNA polymerase)
~structure (keratin, collagen)
~carriers and transport (hemoglobin, aquaporin)
~cell communication (signals and receptors)
~defense (antibodies)
~movement (actin and myosin)
~storage (bean seed)
-structure:
~monomer amino acids
~polymer polypeptide
-can be one or more polypeptide chains folded and bonded together
,-large and complex molecules
-complex 3D shape
amino acids - ✔-structure: central carbon (alpha carbon)
-amino group
-carboxyl group (acid)
-R group (side chain)
~variable group
~different for each
~confers unique chemical properties
-physical and chemical properties based on R groups attached
peptide bonds - ✔-covalent bond between NH2 (amine) of one amino acid and
COOH (carboxyl) of another
-C-N bond
protein structure - ✔-a polypeptide chain that has been folded, twisted and coiled into
unique shapes
-performed as soon as the polypeptide is formed by creating bonds between parts of the chain
-the specific structure determines the function
primary structure - ✔-unique sequence of amino
acids -amino acid sequence determined by gene (DNA)
-slight change in amino acid sequence can affect protein's structure and its function
, secondary structure - ✔-localized folding or pleating of parts of the protein
chain -result of H bonds between repeating structures of polypeptide -weak
bonds
-α helix and β pleated sheets
tertiary structure - ✔-whole molecule folding
-interactions between distant amino acids
-hydrophobic interactions
~cytoplasm is water-based
~nonpolar amino acids cluster away from water
-H bonds and ionic bonds
-disulfide bridges
~covalent bonds between sulfurs in sulfhydryls (S-H)
~anchors 3D shape
quaternary structure - ✔-more than one polypeptide chain bonded
together -only then does polypeptide become functional protein -
hydrophobic interactions
denaturation - ✔-although proteins fold as they are made, under certain conditions,
these proteins will not fold properly
-can be caused by heat, change in pH, change in solution, or salinity
-will be inactive
-some proteins will be able to regain their original structure by removing the elements
nucleic acid - ✔-function: genetic material
-stores information; genes, blueprint for building proteins
