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Final

BIOL 112 Final: Cell & Molecular Biology Final (Schoeck)


Department
Biology
Course Code
BIOL 112
Professor
Joseph Dent
Study Guide
Final

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Macromolecules 4/23/15 5:15 PM
Functional groups
Hydroxyl:
Phosphate:
Sulfhydryl:
Amino:
Carbonyl:
Carboxyl:
Polymers are made up of monomers in condensation reactions
(depolymerization uses hydrolysis)

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Proteins 4/23/15 5:15 PM
Polymers of amino acids
Folding is crucial to the function of a protein and is influenced largely by
sequence of amino acids
Amino Acids:
Nonpolar: glycine, alanine, valine, leucine, isoleucine, methionine,
phenylalanine, tryptophan, proline
Polar: serine, threonine, cysteine, tyrosine, asparagine, glutamine
Negatively Charged: aspartate, glutamate
Positively Charged: lysine, arginine, histidine
Peptide bond formation:
Numbering starts at N (amino) terminus and ends with C (carboxyl)
terminus
Movement is possible on either side of the peptide bond, but not on
the peptide bond due to resonance
Primary structure: made of peptide bonds; forms protein structure
Hydrogen bonds form between peptide chains ! makes secondary protein
structure
Peptide backbone hydrogen bonds determines secondary
structure
α-helix (which are made from coiled coils) and β-pleated sheet
have steady rigid planes, R-groups point outside (can never have
proline as an R-group though)
Coiled coils arise when 2 α-helices have hydrophobic amino acids at
every 4th position (1 turn = 3.6 amino acids)
Tertiary structure is determined by…

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Hydrogen bonding between side chains or between a side chain and
the backbone
Hydrophobic interactions side chains
Disulfide bonds between side chains (made with cysteine)
Ionic bonds between side chains
Every structure is dependent on primary structure
Quaternary structure depend on interactions between R-groups and
between peptide backbones of polypeptides
Since hydrogen bonds are weak, at high temperatures the bonds break and
denature the proteins
Protein turnover (breaking down and resynthesis) occurs constantly and
helps replace broken proteins
Chaperones: specialized proteins that help keep other proteins from
interacting inappropriately with one another by “caging” them in and
releasing them when they’re needed
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