Bio 200 EXAM QUESTIONS WITH COMPLETE
SOLUTIONS!!/GRADE A+ GUARANTEED
SATISFACTION
how to identify potential for hydrogen bond formation between R groups, amino groups and carbonyl
groups - ANSWER-sharing of a hydrogen atom covalently attached to an electronegative element
(typically O-H and N-H groups) between a lone pair of electrons on another electronegative element
impact of different types of mutations on protein structure - ANSWER--Silent mutation: when a
mutation occurs but it has no effect on the protein. multiple codons may result to the same amino acid
Missense mutation: when the substitution results to a different amino acid
Nonsense mutation: when a stop codon replaces what is supposed to be a codon for an amino acid.
When a stop codon is reached, the translation is stopped prematurely and the protein is not formed.
Frameshift mutation: when an extra nucleic acid is inserted or deleted. This has severe effects as it will
not only change one amino acid, but the rest of the remaining amino acids will be affected.
impact of changes in protein structure on function - ANSWER-Gain/change of function: a mutation could
increase the function of a protein, or it could also acquire a new function due to changes in its amino
acid sequence
Loss of function: The change in at a single point could affect the entire function of the protein. For
instance, a single change can remove the ability of a receptor to bind to it. It is also possible that a
change in some residues would change the polarity of the protein, and hence reduce its function.
Nonsense mutations essentially stop protein synthesis prematurely.
coupled reactions - ANSWER-pairs of chemical reactions in which some of the energy released from the
breakdown of one compound is used to create a bond in the formation of another compound
ex. ATP
how does an enzyme increase the rate of a reaction (in terms of activation energy (Ea) and free energy
(deltaG) - ANSWER-they are catalysts, which lowers the activation energy but does not change the free
energy
how chemical properties of amino acids at an enzymes active site affect the rate of a chemical reaction -
ANSWER-may have lower affinity for active site which carries out these functions:
, -Binding Activity: The binding activity is a property of active site which increases the binding affinity of
the substrate with an enzyme.
-Catalytic activity: It is a property of an active site which carries out the catabolic reaction where the
enzyme and substrate react to form a product by reducing the activation energy.
how changes in enzyme structure caused by mutation, temperature, or pH affect the rate of a chemical
reaction - ANSWER--slower reaction above or below ideal pH
-slower reaction above or below ideal temperature. Too high of a temperature and the active site
changes to fit a different amino acid or none at all
Compare and contrast different types of enzyme regulation - ANSWER-competitive inhibition: inhibitor
binds to active site blocking the active site from the substrate
allosteric regulation: a regulatory either has to be present or cannot be present in order for the active
site to be the right shape to accept substrates
R group - ANSWER-An R-group is any group in which the carbon or hydrogen is attached to the rest of
the molecule.
acidic/basic - ANSWER-acidic: low pH
basic: high pH
primary structure - ANSWER--linear sequence of amino acids in a polypeptide chain
-covalent bonds
secondary structure - ANSWER--alpha helix (coil) and beta (pleated sheets) sheets
-H bonds: backbone to backbone
tertiary structure - ANSWER--3d shape
-disulfide bridge: covalent bond b/w sulfur containing R groups
-Hydrogen bonds: R group to R group AND R group to backbone
-Hydrophobic interactions
SOLUTIONS!!/GRADE A+ GUARANTEED
SATISFACTION
how to identify potential for hydrogen bond formation between R groups, amino groups and carbonyl
groups - ANSWER-sharing of a hydrogen atom covalently attached to an electronegative element
(typically O-H and N-H groups) between a lone pair of electrons on another electronegative element
impact of different types of mutations on protein structure - ANSWER--Silent mutation: when a
mutation occurs but it has no effect on the protein. multiple codons may result to the same amino acid
Missense mutation: when the substitution results to a different amino acid
Nonsense mutation: when a stop codon replaces what is supposed to be a codon for an amino acid.
When a stop codon is reached, the translation is stopped prematurely and the protein is not formed.
Frameshift mutation: when an extra nucleic acid is inserted or deleted. This has severe effects as it will
not only change one amino acid, but the rest of the remaining amino acids will be affected.
impact of changes in protein structure on function - ANSWER-Gain/change of function: a mutation could
increase the function of a protein, or it could also acquire a new function due to changes in its amino
acid sequence
Loss of function: The change in at a single point could affect the entire function of the protein. For
instance, a single change can remove the ability of a receptor to bind to it. It is also possible that a
change in some residues would change the polarity of the protein, and hence reduce its function.
Nonsense mutations essentially stop protein synthesis prematurely.
coupled reactions - ANSWER-pairs of chemical reactions in which some of the energy released from the
breakdown of one compound is used to create a bond in the formation of another compound
ex. ATP
how does an enzyme increase the rate of a reaction (in terms of activation energy (Ea) and free energy
(deltaG) - ANSWER-they are catalysts, which lowers the activation energy but does not change the free
energy
how chemical properties of amino acids at an enzymes active site affect the rate of a chemical reaction -
ANSWER-may have lower affinity for active site which carries out these functions:
, -Binding Activity: The binding activity is a property of active site which increases the binding affinity of
the substrate with an enzyme.
-Catalytic activity: It is a property of an active site which carries out the catabolic reaction where the
enzyme and substrate react to form a product by reducing the activation energy.
how changes in enzyme structure caused by mutation, temperature, or pH affect the rate of a chemical
reaction - ANSWER--slower reaction above or below ideal pH
-slower reaction above or below ideal temperature. Too high of a temperature and the active site
changes to fit a different amino acid or none at all
Compare and contrast different types of enzyme regulation - ANSWER-competitive inhibition: inhibitor
binds to active site blocking the active site from the substrate
allosteric regulation: a regulatory either has to be present or cannot be present in order for the active
site to be the right shape to accept substrates
R group - ANSWER-An R-group is any group in which the carbon or hydrogen is attached to the rest of
the molecule.
acidic/basic - ANSWER-acidic: low pH
basic: high pH
primary structure - ANSWER--linear sequence of amino acids in a polypeptide chain
-covalent bonds
secondary structure - ANSWER--alpha helix (coil) and beta (pleated sheets) sheets
-H bonds: backbone to backbone
tertiary structure - ANSWER--3d shape
-disulfide bridge: covalent bond b/w sulfur containing R groups
-Hydrogen bonds: R group to R group AND R group to backbone
-Hydrophobic interactions
