BCH4024 EXAM 1 QUESTIONS
WITH ALL CORRECT ANSWERS
GRADED A+
When we have 1/4 of the tetramers filled with CO, the other 3/4 go on with --------, so we
get pO2 that is 75%, but this is -------observed, this is why the hemoglobin ------follow
the sequential model - Answer- cooperativity, never, does not
When we have 1/4 of the tetramers filled with CO, the first change in G from R0-R1 is ---
-------than the ones that follower, which are all the same (change). REMEMBER, this is
not observed because hemoglobin follows ONLY the concerted model - Answer- larger
At higher elevations, we have reduced O2, lactic acid lowers blood PH. This trigger ------
------ synthesis by RBC - Answer- 2,3 BPG
The 2,3 BPG ---------deoxy hemoglobin, favoring ---------dissociation and eventual
release to tissues, this is restored when you return down to normal conditions - Answer-
stabilizes, O2
2,3 BPG binds to the hole in the ----------state, making it more ------, which means harder
to get O2 to -------and easier to release - Answer- T, stable, bind
Hemoglobin releases --------O2 at low Ph - Answer- more
Bohr effect: how O2 --------H+ binding and vice versa. When there is less O2, there is
acid build up, this lowers the PH, the s curve shifts to the right because pO2 is less -
Answer- antagonizes
When you less O2, the T state, which has no affinity for O2 is more stable, your PH
lowers, this means we get rid of --------O2 - Answer- more
In other words, when hemoglobin is protonated, it stabilizes the -------state favoring
deoxygenation - Answer- T
Additional ----------are released to further stabilize the T state, when CO2 hydration
binds to N terminal of hemoglobin. The reaction for this follows that CO2 and water form
biocarbonate, which splits into its depronated form - Answer- protons
When the CO2 is on the right side of the equation, you know that we have a hemoglobin
that has reached the ------ - Answer- lungs
,Enzymes are the verbs in biological reactions, play a central role in biochemical
processes. They increase reaction ------without altering ----- - Answer- rates, equilibria
Enzymatic activity operate billions of times faster and can be -------- - Answer- regulated
Why are most enzymes proteins not RNA, they are more ------- that way. The few
ribozymes are leftovers from evolution - Answer- flexible
One reason why we study enzymes is to --------- them in other to make highly effective
drugs - Answer- inhibit
Enzyme classes- those that catalyze oxidation reductive reactions are known as ----------
. An example is ---------- on NAD+ - Answer- oxidoreductases, alcohol dehydrogenase
Enzyme classes- those that catalyze the transfer of functional groups are known as -----
----, an example is hexokinase on glucose - Answer- transferases
Enzyme classes- those that catalyze the hydration of covalent bonds are known as-------
-----. An example is ----------- - Answer- hydrolases, glucose 6 phosphate
Enzyme classes- those that catalyze the elimination/ addition of functional groups are
known as-----------. An example is -------- - Answer- lyases, fumarase
Enzyme classes- those that catalyze intramolecular rearrangements are known as--------
----. An example is ----------- - Answer- isomerases(isomers), phosphoglucoisomerase
Enzyme classes- those that catalyze the joining of molecules are known as ----------. An
example is ----- - Answer- ligases, glutamine synthetase
Enzyme classes- those that convert chemical bond energy to mechanical energy are
known as-------------. An example is the --------- - Answer- energases, actomyosin
The AA's that would be nucleophilic for enzymes are - Answer- lysine, histidine,
cysteine and serine
Enzymes can be conjugated with inorganic conjugates--------- and organic conjugates
like vitamins & NAD+---------- - Answer- cofactors, coenzymes
It is important to note that enzymes always return to their -------states - Answer- original
ATP tends to bind to which amino acid? - Answer- arginine
Cofactors bind ---------- (fashion)to --------(type)ions - Answer- reversibly, metal
----------group tightly bind to molecules, and examples are metals - Answer- Prosthetic
, Some coenzymes are bound and released as ------- - Answer- cosubstrates
Limited size of active sites (stereospecific) keeps binding energy in a ---------, perfect
state - Answer- Goldilocks state
Chymotrypsin tends to cleave -------chains. And --------glucose is the most common
sugar - Answer- long, D
----------- transition state in enzyme catalysis means that substrate and enzyme change
simultaneously - Answer- Joint
The joint transition state is also very ------------, lasting for very short period of time -
Answer- transient
The active site of the enzyme will almost always do everything it can to -----------
reactivity - Answer- promote
Enzymes love to make work easier, they like to go through the -------of the energy
barriers, they are therefore said to be ------- - Answer- valleys, syncatalytic
In an uncatalyzed reaction, the delta G is --------- than zero - Answer- greater
In an enzyme catalyzed reaction, forward and backwards rates increase by the -----------
-factor - Answer- same
Velocity of a reaction is defined as the concentration change per - Answer- second
For first order reaction, velocity depends only on ---------OR ------ - Answer- reactants,
products
----------theory talks about reaction rate in relation to ------------barrier height - Answer-
Absolute, energy
The higher the energy barrier, the slower the --------of the reaction - Answer- rate
The ---------frequency of a chemical bond is the fastest that a rxn can go - Answer-
vibrational
The larger the delta G, the slower the -------- - Answer- rate constant (k)
--------energy is the energy released in the substrate enzyme interaction - Answer-
Binding
Substrate specificity relies on ----------interactions, which in the transition state are --------
--than the ES complex - Answer- noncovalent, stronger
WITH ALL CORRECT ANSWERS
GRADED A+
When we have 1/4 of the tetramers filled with CO, the other 3/4 go on with --------, so we
get pO2 that is 75%, but this is -------observed, this is why the hemoglobin ------follow
the sequential model - Answer- cooperativity, never, does not
When we have 1/4 of the tetramers filled with CO, the first change in G from R0-R1 is ---
-------than the ones that follower, which are all the same (change). REMEMBER, this is
not observed because hemoglobin follows ONLY the concerted model - Answer- larger
At higher elevations, we have reduced O2, lactic acid lowers blood PH. This trigger ------
------ synthesis by RBC - Answer- 2,3 BPG
The 2,3 BPG ---------deoxy hemoglobin, favoring ---------dissociation and eventual
release to tissues, this is restored when you return down to normal conditions - Answer-
stabilizes, O2
2,3 BPG binds to the hole in the ----------state, making it more ------, which means harder
to get O2 to -------and easier to release - Answer- T, stable, bind
Hemoglobin releases --------O2 at low Ph - Answer- more
Bohr effect: how O2 --------H+ binding and vice versa. When there is less O2, there is
acid build up, this lowers the PH, the s curve shifts to the right because pO2 is less -
Answer- antagonizes
When you less O2, the T state, which has no affinity for O2 is more stable, your PH
lowers, this means we get rid of --------O2 - Answer- more
In other words, when hemoglobin is protonated, it stabilizes the -------state favoring
deoxygenation - Answer- T
Additional ----------are released to further stabilize the T state, when CO2 hydration
binds to N terminal of hemoglobin. The reaction for this follows that CO2 and water form
biocarbonate, which splits into its depronated form - Answer- protons
When the CO2 is on the right side of the equation, you know that we have a hemoglobin
that has reached the ------ - Answer- lungs
,Enzymes are the verbs in biological reactions, play a central role in biochemical
processes. They increase reaction ------without altering ----- - Answer- rates, equilibria
Enzymatic activity operate billions of times faster and can be -------- - Answer- regulated
Why are most enzymes proteins not RNA, they are more ------- that way. The few
ribozymes are leftovers from evolution - Answer- flexible
One reason why we study enzymes is to --------- them in other to make highly effective
drugs - Answer- inhibit
Enzyme classes- those that catalyze oxidation reductive reactions are known as ----------
. An example is ---------- on NAD+ - Answer- oxidoreductases, alcohol dehydrogenase
Enzyme classes- those that catalyze the transfer of functional groups are known as -----
----, an example is hexokinase on glucose - Answer- transferases
Enzyme classes- those that catalyze the hydration of covalent bonds are known as-------
-----. An example is ----------- - Answer- hydrolases, glucose 6 phosphate
Enzyme classes- those that catalyze the elimination/ addition of functional groups are
known as-----------. An example is -------- - Answer- lyases, fumarase
Enzyme classes- those that catalyze intramolecular rearrangements are known as--------
----. An example is ----------- - Answer- isomerases(isomers), phosphoglucoisomerase
Enzyme classes- those that catalyze the joining of molecules are known as ----------. An
example is ----- - Answer- ligases, glutamine synthetase
Enzyme classes- those that convert chemical bond energy to mechanical energy are
known as-------------. An example is the --------- - Answer- energases, actomyosin
The AA's that would be nucleophilic for enzymes are - Answer- lysine, histidine,
cysteine and serine
Enzymes can be conjugated with inorganic conjugates--------- and organic conjugates
like vitamins & NAD+---------- - Answer- cofactors, coenzymes
It is important to note that enzymes always return to their -------states - Answer- original
ATP tends to bind to which amino acid? - Answer- arginine
Cofactors bind ---------- (fashion)to --------(type)ions - Answer- reversibly, metal
----------group tightly bind to molecules, and examples are metals - Answer- Prosthetic
, Some coenzymes are bound and released as ------- - Answer- cosubstrates
Limited size of active sites (stereospecific) keeps binding energy in a ---------, perfect
state - Answer- Goldilocks state
Chymotrypsin tends to cleave -------chains. And --------glucose is the most common
sugar - Answer- long, D
----------- transition state in enzyme catalysis means that substrate and enzyme change
simultaneously - Answer- Joint
The joint transition state is also very ------------, lasting for very short period of time -
Answer- transient
The active site of the enzyme will almost always do everything it can to -----------
reactivity - Answer- promote
Enzymes love to make work easier, they like to go through the -------of the energy
barriers, they are therefore said to be ------- - Answer- valleys, syncatalytic
In an uncatalyzed reaction, the delta G is --------- than zero - Answer- greater
In an enzyme catalyzed reaction, forward and backwards rates increase by the -----------
-factor - Answer- same
Velocity of a reaction is defined as the concentration change per - Answer- second
For first order reaction, velocity depends only on ---------OR ------ - Answer- reactants,
products
----------theory talks about reaction rate in relation to ------------barrier height - Answer-
Absolute, energy
The higher the energy barrier, the slower the --------of the reaction - Answer- rate
The ---------frequency of a chemical bond is the fastest that a rxn can go - Answer-
vibrational
The larger the delta G, the slower the -------- - Answer- rate constant (k)
--------energy is the energy released in the substrate enzyme interaction - Answer-
Binding
Substrate specificity relies on ----------interactions, which in the transition state are --------
--than the ES complex - Answer- noncovalent, stronger
