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AP Biology Chapter 1 Test Guide with Questions Solved 100% Correct $12.99   Add to cart

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AP Biology Chapter 1 Test Guide with Questions Solved 100% Correct

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  • Course
  • AP Biology
  • Institution
  • AP Biology

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 an...

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  • August 28, 2024
  • 16
  • 2024/2025
  • Exam (elaborations)
  • Questions & answers
  • AP Biology
  • AP Biology
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KenAli
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

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