Exam 1 - BIO 200 – UW Questions with
Complete Solutions
phosphate - ANSWER-linked together, these store a lot of potential energy due to
the electrons on the phosphate groups crowding (electron repulsion)
sulfhydryl - ANSWER-thiols; when present in proteins, can form S-S bonds to form
proteins
PROTEINS AND ENZYMES - ANSWER-
macromolecule - ANSWER-a very large molecule made up of smaller molecules
joined together (aka polymers)
Why R-groups are important - ANSWER-They enable tertiary structure - R group
interactions cause further folding (after secondary structures have formed) and
contribute to the overall globular protein shape. Also they are what make each amino
acid different
molecular chaperones - ANSWER-proteins that facilitate folding in cells- part of the
heat-shock proteins
heat-shock proteins - ANSWER-produced after cells experience high
temperatures/anything that undos tertiary structure. they bind to hydrophobic
patches that otherwise wouldn't be exposed; allows proteins to re-fold
saturation kinetics - ANSWER-even with increased substrate amounts, active sites of
enzymes can only take a certain maximum of substrates in a reaction at the fastest
rate that they can
cofactors - ANSWER-inorganic ions that interact with enzymes
coenzymes - ANSWER-organic molecules that reversibly interact with enzymes,
such as electron carriers NADH or FADH2
prosthetic groups - ANSWER-non-amino acid atoms/molecules that are permenantly
attached to proteins
induced fit - ANSWER-change in chape of an enzyme that occurs when a substrate
binds to the active site.
competitive inhibition - ANSWER-regulatory molecule inhibits substrates from
accessing the active site
, allosteric regulation - ANSWER-another molecule binds on to the enzyme (but not on
the active site), changing its shape so that its function is also changed
primary structure - ANSWER-The sequence of amino acids in a protein
secondary structure - ANSWER-Amino-carboxy backbone interactions cause folding
in certain ways (examples of this include a-helices and ß-pleated sheets)
tertiarty structure - ANSWER-R-group interactions cause further folding to contribute
to the overall globular protein shape
quaternary structure - ANSWER-Interactions between 2 or more proteins
ligand - ANSWER-Any molecule that binds to a specific site on a receptor molecule.
voltage-gating - ANSWER-opens as the cell polarizes or depolarizes to a specific
voltage
activation energy - ANSWER-energy required for a reaction to occur
transition state - ANSWER-temporary unstable intermediate condition where the
degree of interaction between enzyme and substrate increases and reaches a
maximum
energetic coupling - ANSWER-chemical energy released from one reaction allows
another to take place (usually by adding ATP to an otherwise endergonic reaction).
This actually changed the reaction over all. Page 144 shows this pretty well; instead
of A and B trying to react via an endergonic reaction, ATP, A, and B are all reacting
(thus, different reactants make for a different chemical reaction). Also, this process is
energetically favorable because the resulting ADP has less potential energy, making
it more stable as a molecule.
CHEMISTRY TO KNOW... SERIOUSLY - ANSWER-
hydrogen bonding - ANSWER-a bond between two molecules resulting from an
electrostatic attraction between a proton in one molecule and an electronegative
atom in the other
van de waals forces - ANSWER-transient attraction between atoms when there is a
tinnnnnny negative charge on one and a tinnnnyyy positive charge on another, which
very slightly and very quickly attract each other. This is possible since electrons are
always moving around in a random manner
hydrophobic interaction - ANSWER-non-polar interactions (same as van der waals
forces)
ionic bonding - ANSWER-Full charge interactions
covalent bonding - ANSWER-Sharing of electrons between 2 nuclei
Complete Solutions
phosphate - ANSWER-linked together, these store a lot of potential energy due to
the electrons on the phosphate groups crowding (electron repulsion)
sulfhydryl - ANSWER-thiols; when present in proteins, can form S-S bonds to form
proteins
PROTEINS AND ENZYMES - ANSWER-
macromolecule - ANSWER-a very large molecule made up of smaller molecules
joined together (aka polymers)
Why R-groups are important - ANSWER-They enable tertiary structure - R group
interactions cause further folding (after secondary structures have formed) and
contribute to the overall globular protein shape. Also they are what make each amino
acid different
molecular chaperones - ANSWER-proteins that facilitate folding in cells- part of the
heat-shock proteins
heat-shock proteins - ANSWER-produced after cells experience high
temperatures/anything that undos tertiary structure. they bind to hydrophobic
patches that otherwise wouldn't be exposed; allows proteins to re-fold
saturation kinetics - ANSWER-even with increased substrate amounts, active sites of
enzymes can only take a certain maximum of substrates in a reaction at the fastest
rate that they can
cofactors - ANSWER-inorganic ions that interact with enzymes
coenzymes - ANSWER-organic molecules that reversibly interact with enzymes,
such as electron carriers NADH or FADH2
prosthetic groups - ANSWER-non-amino acid atoms/molecules that are permenantly
attached to proteins
induced fit - ANSWER-change in chape of an enzyme that occurs when a substrate
binds to the active site.
competitive inhibition - ANSWER-regulatory molecule inhibits substrates from
accessing the active site
, allosteric regulation - ANSWER-another molecule binds on to the enzyme (but not on
the active site), changing its shape so that its function is also changed
primary structure - ANSWER-The sequence of amino acids in a protein
secondary structure - ANSWER-Amino-carboxy backbone interactions cause folding
in certain ways (examples of this include a-helices and ß-pleated sheets)
tertiarty structure - ANSWER-R-group interactions cause further folding to contribute
to the overall globular protein shape
quaternary structure - ANSWER-Interactions between 2 or more proteins
ligand - ANSWER-Any molecule that binds to a specific site on a receptor molecule.
voltage-gating - ANSWER-opens as the cell polarizes or depolarizes to a specific
voltage
activation energy - ANSWER-energy required for a reaction to occur
transition state - ANSWER-temporary unstable intermediate condition where the
degree of interaction between enzyme and substrate increases and reaches a
maximum
energetic coupling - ANSWER-chemical energy released from one reaction allows
another to take place (usually by adding ATP to an otherwise endergonic reaction).
This actually changed the reaction over all. Page 144 shows this pretty well; instead
of A and B trying to react via an endergonic reaction, ATP, A, and B are all reacting
(thus, different reactants make for a different chemical reaction). Also, this process is
energetically favorable because the resulting ADP has less potential energy, making
it more stable as a molecule.
CHEMISTRY TO KNOW... SERIOUSLY - ANSWER-
hydrogen bonding - ANSWER-a bond between two molecules resulting from an
electrostatic attraction between a proton in one molecule and an electronegative
atom in the other
van de waals forces - ANSWER-transient attraction between atoms when there is a
tinnnnnny negative charge on one and a tinnnnyyy positive charge on another, which
very slightly and very quickly attract each other. This is possible since electrons are
always moving around in a random manner
hydrophobic interaction - ANSWER-non-polar interactions (same as van der waals
forces)
ionic bonding - ANSWER-Full charge interactions
covalent bonding - ANSWER-Sharing of electrons between 2 nuclei
