Biochemistry Review for OA - WGU
Comprehensive Questions (Frequently
Tested) with Verified Answers Graded A+
polar amino acids - Answer: - polar bears like water!
- OH, NH, SH, or use S.O.N.
nonpolar amino acids - Answer: - hydrophobic
- CH (can't have water)
- look for CH, CH2, CH3
ionized amino acids - Answer: the charged amino acids +/- attached to them.
alanine - Answer: - is hydrophobic, has CH3 as its weak interaction
neurodegenerative protein aggregation - Answer: misfolding of a protein structure in
alzheimer's disease the most common neurodegenerative disease.
- caused by intracellular tangles and extracellular plaques caused by ABNORMAL PROTEIN
AGGREGATION
chaperones - Answer: molecules that help denatured proteins in folding (they help newly
formed proteins and can also help the misfolded ones)
primary protein structure - Answer: chain of amino acids, peptide bonds forming a polypeptide
chain; BACKBONE
- covalent bond: strong and does not denature
,what structure would be UNAFFECTED by complete denaturation of multi-subunit? - Answer:
PRIMARY, peptide bonds are strong and covalent. primary formed by peptide bonds.
what level of protein structure is disrupted through the hydrolysis of peptide bonds and formed
by dehydration reactions? - Answer: PRIMARY
secondary protein structure - Answer: alpha helix and beta sheets. held together by hydrogen
bond. denatured by salt and pH change. carboxyl group and amino group
*hydrogen bonds formed from 2 polar amino acids
tertiary protein structure - Answer: 3-D shape (sickle cell, arthritis, hemophilia). changes seen
with increased temperature, salt, change in pH, and reducing agents.
- hydrophobic, found on inside, protein structure is stabilized primarily by the hydrophobic
effect, disruption of the hydrophobic effect is the simplest way to denature- which is done by
increased temp from heating up
- has to do with side chains
quarternary protein structure - Answer: more than one polypeptide or subunit held by
hydrophobic interactions, hydrogen bonds, ionic bonds, disulfide bonds (side chain)
- HgB changes seen with increased temperature
LOSE FORM = ? - Answer: LOSE FUNCTION
dehydration synthesis - Answer: water is removed
hydrolysis - Answer: water is added
peptide bond - Answer: form between 2 amino acids via DEHYDRATION reaction. during the
reaction, a water molecule forms from the oxygen of a carboxyl group and 2 hydrogens from an
, amino group. as water forms, the carbon atom of the carboxyl group and the nitrogen atom of
the amino group become bonded together. this bond between the two amino acids is called a ?
methotrexate treatment in cancer - Answer: works by blocking an enzyme process in cancer
cells so that they cannot grow
induced fit - Answer: enzyme giving substrate a big hug!
- many enzymes will adjust their active site conformation slightly as the substrate binds to
improve the fit --> when the molecule is recognized as the substrate, the enzyme will adjust to
form itself around the substrate more tightly to facilitate a rxn --> catalyzes
enzyme-substrate complex - Answer: each substrate binds to an active site which produces this
substrate - Answer: molecule that an enzyme will bind preferentially to any other molecule.
each enzyme is specific for that substrate, it won't react with molecules that are not its own
substrate. increase substrate increase rxns
active site - Answer: enzymes have an active site, which serves as the binding platform for its
specific substrates and acts as the site of the chemical reaction
allosteric site - Answer: any site OTHER THAN the active site
substrate/enzymes/active site - Answer: - substrate enters active site of enzyme
- enzyme/substrate complex slight change in shape
- enzyme/products complex change in color
- product released
enzyme catalyze a reaction - Answer: 1. substrate recognition
Comprehensive Questions (Frequently
Tested) with Verified Answers Graded A+
polar amino acids - Answer: - polar bears like water!
- OH, NH, SH, or use S.O.N.
nonpolar amino acids - Answer: - hydrophobic
- CH (can't have water)
- look for CH, CH2, CH3
ionized amino acids - Answer: the charged amino acids +/- attached to them.
alanine - Answer: - is hydrophobic, has CH3 as its weak interaction
neurodegenerative protein aggregation - Answer: misfolding of a protein structure in
alzheimer's disease the most common neurodegenerative disease.
- caused by intracellular tangles and extracellular plaques caused by ABNORMAL PROTEIN
AGGREGATION
chaperones - Answer: molecules that help denatured proteins in folding (they help newly
formed proteins and can also help the misfolded ones)
primary protein structure - Answer: chain of amino acids, peptide bonds forming a polypeptide
chain; BACKBONE
- covalent bond: strong and does not denature
,what structure would be UNAFFECTED by complete denaturation of multi-subunit? - Answer:
PRIMARY, peptide bonds are strong and covalent. primary formed by peptide bonds.
what level of protein structure is disrupted through the hydrolysis of peptide bonds and formed
by dehydration reactions? - Answer: PRIMARY
secondary protein structure - Answer: alpha helix and beta sheets. held together by hydrogen
bond. denatured by salt and pH change. carboxyl group and amino group
*hydrogen bonds formed from 2 polar amino acids
tertiary protein structure - Answer: 3-D shape (sickle cell, arthritis, hemophilia). changes seen
with increased temperature, salt, change in pH, and reducing agents.
- hydrophobic, found on inside, protein structure is stabilized primarily by the hydrophobic
effect, disruption of the hydrophobic effect is the simplest way to denature- which is done by
increased temp from heating up
- has to do with side chains
quarternary protein structure - Answer: more than one polypeptide or subunit held by
hydrophobic interactions, hydrogen bonds, ionic bonds, disulfide bonds (side chain)
- HgB changes seen with increased temperature
LOSE FORM = ? - Answer: LOSE FUNCTION
dehydration synthesis - Answer: water is removed
hydrolysis - Answer: water is added
peptide bond - Answer: form between 2 amino acids via DEHYDRATION reaction. during the
reaction, a water molecule forms from the oxygen of a carboxyl group and 2 hydrogens from an
, amino group. as water forms, the carbon atom of the carboxyl group and the nitrogen atom of
the amino group become bonded together. this bond between the two amino acids is called a ?
methotrexate treatment in cancer - Answer: works by blocking an enzyme process in cancer
cells so that they cannot grow
induced fit - Answer: enzyme giving substrate a big hug!
- many enzymes will adjust their active site conformation slightly as the substrate binds to
improve the fit --> when the molecule is recognized as the substrate, the enzyme will adjust to
form itself around the substrate more tightly to facilitate a rxn --> catalyzes
enzyme-substrate complex - Answer: each substrate binds to an active site which produces this
substrate - Answer: molecule that an enzyme will bind preferentially to any other molecule.
each enzyme is specific for that substrate, it won't react with molecules that are not its own
substrate. increase substrate increase rxns
active site - Answer: enzymes have an active site, which serves as the binding platform for its
specific substrates and acts as the site of the chemical reaction
allosteric site - Answer: any site OTHER THAN the active site
substrate/enzymes/active site - Answer: - substrate enters active site of enzyme
- enzyme/substrate complex slight change in shape
- enzyme/products complex change in color
- product released
enzyme catalyze a reaction - Answer: 1. substrate recognition
