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WorksheetsChem 1421 midterm
Total questions: 124
Worksheet time: 1hrs 2mins
Which of the following is not true?
Molecular oxygen is always a substrate in oxidation reactions.
Oxidation reactions involve the movement of electrons from one molecule to another
When a molecule is oxidized, it loses electrons
Reduction involves the gain of electrons
The information needed for the structure of a protein is contained in
amino acid composition
primary structure
secondary structure
tertiary structure
Exhibit 2A
The structure of ATP with various groups labeled.
Group III is the entire phosphate group.
Refer to Exhibit 2A. Which of the groups could not act as a proton acceptor in a hydrogen bond?
I
II
III
IV
All can accept a hydrogen in a hydrogen bond
Exhibit 4A.
The following question(s) refer to this peptide:
Cys-Ala-Gly-Arg-Gln-Met
Refer to Exhibit 4A. The overall, net ionic charge on this peptide at pH = 7 would be:
+2
+1
0
-1
-2
Iron deficiency in a cell can adversely affect electron transport at which of the following sites?
coenzyme Q and FADH2
NADH and FADH2
cytochrome b and cytochrome c
coenzyme Q and NADH
Complex IV of the electron transport chain oxidizes ____, reduces ____, and ____ protons in the process.
coenzyme Q; cytochrome c; pumps
cytochrome c; coenzyme Q; pumps
cytochrome c; O2; doesn't pump
cytochrome c; O2; pumps
Which of the following terms describes ATP synthesis in mitochondria?
substrate-level phosphorylation
oxidative phosphorylation
photophosphorylation
none of these
A characteristic of the glycerol phosphate shuttle is
It shuttles NADH across the mitochondrial membrane to yield 2.5 ATP/ADH.
It shuttles "NADH electron equivalents" across the mitochondrial membrane to yield 1.5 ATP/NADH.
It only operates efficiently when the [NADH] in the cytoplasm is higher than in the matrix.
Malate is a key component in the shuttle process.
The only reaction which actually uses molecular oxygen is
Cytochrome C oxidase.
NADH-CoQ reductase.
succinate-CoQ reductase.
Cytochrome A oxidase.
Cytochrome bc1 complex.
In order to drive the synthesis of ATP, the hydrolysis of an organic phosphate
must have a higher free energy change.
must have a lower free energy change.
must have a free energy change equal to that of ATP.
In a hydrogen bond
three atoms lie in a straight line
there is stronger bonding than in a covalent bond
unpaired electrons play no role
none of the above
Complex II of the electron transport chain oxidizes ____, reduces ____, and ____ protons in the process.
FADH2; coenzyme Q; doesn't pump
FADH2; coenzyme Q; pumps
NADH; coenzyme Q; doesn't pump
NADH; coenzyme Q; pumps
Which of the following is not true?
A buffer is a solution which maintains a solution at a neutral pH
Buffer solutions are made to resist change in pH
Zwitterion buffers are less likely to interfere with biological reactions than non-zwitterions
HEPES is a zwitterion buffer
The hydrolysis of ATP can be used to drive reactions that have a DG' that is
greater than +5 kJ/mol
less than +5 kJ/mol
between +20 and +40 kJ/mol
not possible to determine from the information in this chapter
Which of the following are located in the inner mitochondrial membrane?
all the components of the citric acid cycle and the electron transport chain
all the components of the citric acid cycle but none of the components of the electron transport chain
all the components of the electron transport chain but none of the components of the citric acid cycle
all the components of the electron transport chain and one of the components of the citric acid cycle, namely the succinate dehydrogenase complex
When we say that the efficiency of glycolysis is about 33% we mean that
2 ATP are produced and 6 ATP are involved in the overall process
2 ATP are produced in the oxidation of glucose, which contains six carbon atoms
the energy used to phosphorylate 2 ATP is 33% of the energy released in the process
all of these
Which of the following is not true?
The heme group of myoglobin is held in place only through non-covalent bonding.
The F8 histidine is important to the function of myoglobin
The E7 histidine is important to the function of myoglobin
Myoglobin and hemoglobin differ only in one amino acid
Which of the following statements apply to anabolism?
proceeds in stages
requires energy
requires reducing agents
all of these
Which complex contains succinate dehydrogenase?
Complex I
Complex II
Complex III
Complex IV
It is not known where succinate dehydrogenase is located.
What would happen to hemoglobin if the BPG were removed?
It would not bind oxygen
It would dissociate into monomers
its oxygen binding curve would resemble that of myoglobin
all of the choices
Exhibit 2B Contains information of the pK's of some common buffers.
Refer to Exhibit 2B. An ammonium buffer would work well at this pH
5.6
7.0
9.0
11.0
none of these
Incorrect protein folding resulting in exposure of hydrophobic regions can result in
aggregation
homology
liposomes
the Bohr effect.
The phosphorylation of ADP to produce ATP is endergonic because
a negatively charged ion is bonded to a molecule that already carries a negative charge
ATP is more stable than ADP
the entropy of the products is less than that of the reactants
polyphosphate chains are the storage form of phosphorus in living organisms
A buffer solution at pH 10 has a ratio of [HA]/[A-] of 10. What is the pKa of the acid?
8
9
10
11
12
Adult hemoglobin is half saturated with oxygen at what partial pressure of oxygen?
5 torr
10 torr
25 torr
50 torr
100 torr
Uncoupling in mitochondria refers to:
Interruption of electron flow.
Stopping electron flow but not stopping ATP synthesis.
Stopping ATP synthesis but not stopping electron flow.
Blocking the electrons from NADH from entering the electron transport system.
All of these describe uncoupling.
Which of the following best describes what happens when hemoglobin binds bisphosphoglyceric acid (BPG)?
Binding of BPG leads to tighter binding of oxygen.
Binding of BPG allows maternal (adult) Hb to bind oxygen more tightly than fetal Hb.
Binding of BPG is important to the allosteric nature of hemoglobin
Binding of BPG causes the subunits of hemoglobin to separate.
Which of the following is not true of the process of oxidative phosphorylation?
protons flow into the mitochondrial matrix through ion channels in the ATP synthase
the F0 part of the ATP synthase serves as a proton channel
the F1 part of the ATP synthase is the site of ATP formation
iron-sulfur proteins bind to the ATP synthase
Exhibit 4A
The following question(s) refer to this peptide:
Cys-Ala-Gly-Arg-Gln-Met
Refer to Exhibit 4A. The carboxyl terminal end is
Arg
Cys
Gln
Met
None of these
Exhibit 2 BContains information on the pk's of some common buffers.Refer to exhibit 2 B. A phosphate buffer would work well with this ph
5.0
7.0
8.0
10.0
7.0 and 8.0
Which of the following is true?
The collagen helix and the a-helix are the only types of helices in proteins.
Globular proteins tend to be water soluble
Globular and fibrous are examples of secondary structure
All of these
The binding of oxygen to hemoglobin differs from the oxygen-binding behavior of myoglobin because
oxygen binding to hemoglobin is cooperative.
oxygen binding to myoglobin is cooperative.
hemoglobin is not an allosteric protein.
the oxygen-binding curve of hemoglobin is hyperbolic.
Consider a reaction that produces a significant amount of hydrogen ion and is to be carried out a pH 7. Only two acids are available for making the buffer solution. The pKa values for acids A and B are 6.3 and 7.3, respectively. Which acid would serve as the optimum buffer for this reaction? Or would carrying out the reaction in water simply serve as well?
Acid A
Acid B
water
both acids would be equally effective
Which of the following statements regarding hemoglobin (Hb) and myoglobin (Mb) is true?
Mb transports oxygen while Hb stores it.
Mb has quaternary structure but Hb does not.
Mb displays simple kinetics of binding while Hb displays cooperativity.
Mb binds Fe(II) while Hb binds heme.
Which of the following elements has the highest electronegativity?
C
H
N
O
P
What happens to the entropy of a molecule as the number of resonance structures increases?
Entropy also increases.
Entropy decreases.
Entropy has no relationship to the number of resonance
Hydrogen bonds explain which of the following properties of water?
Water is a great solvent for all ionic and polar molecules.
Water has high melting and boiling points for its small size.
Ice expands when frozen.
Both the abnormal melting and freezing points and that ice expands when frozen.
Hydrogen bonds explain all of these properties.
Chemiosmotic coupling involves this process:
Using an electron gradient to synthesize ATP.
Using a proton gradient to synthesize ATP.
Using oxygen flow to synthesize ATP.
Using a proton gradient to make water from oxygen.
These are all chemiosmotic processes.
Which of the following principles states that if stress is applied to a system in equilibrium, the equilibrium will shift in the direction that relieves the stress?
Pauli exclusion principle
Mach's principle
Fermat's principle
Le Chatelier's principle
Which of the following amino acid substitutions would be least likely to have a deleterious effect on protein function?
His changes to Asp
Leu changes to Ile
Glu changes to Gln
Trp changes to Gly
The following bond forces are important in quaternary structure
Disulfide bonds
Hydrogen bonds
Hydrophobic attraction
Both hydrogen bonds and hydrophobic attraction.
An alternative mode of entry into the electron transport chain is the oxidation of
malate to oxalosuccinate.
succinate to fumarate.
isocitrate to a-ketoglutarate.
a-ketoglutarate to succinyl-CoA.
Which substance would be the best buffer at pH 8 if it had to be able to buffer against either acid or base?
one with a pKa of 7
one with a pKa of 8
one with a pKa of 9
The pKa of a substance doesn't tell you whether it would be a good buffer at this pH.
Variations in the structure of hemoglobin
do not always have an adverse effect on health
can alter the binding of heme to the protein
can occur on the surface of the protein
all of these
In general, catabolism
is an oxidative process that releases energy
is a reductive process that releases energy
is an oxidative process that requires energy
is a reductive process that requires energy
none of these
The reference reaction for determining reduction potentials (E = 0) is the reduction of
oxygen (O2) to water.
NAD+ to NADH.
H+ to H2 gas.
FAD to FADH2.
Spontaneous reaction always occurs at a relatively fast rate.
True
False
In general, catabolism
releases energy.
absorbs energy.
neither absorbs nor releases energy.
The dissociation constant for an acid is 1 x 10-6. What is its pKa?
-6
6
0.6
-0.6
If a solution has a pH = 6, the [H+] is
6M
106M
10-6M
0.6M
I am performing a reaction, A ® B, with DG' = -0.3 kJ/mol. I start the reaction with 10 mM A and no B. After allowing the reaction to proceed for 24 hrs at room temperature and atmospheric pressure, I analyze a sample of the reaction mix to find I now have 1 mM A and 9 mM B. Which of the following conclusions should I make?
The reaction has reached equilibrium.
I should come back again later; equilibrium has not yet been reached.
The formation of B from A is thermodynamically unfavorable, so I should find another starting material to make B.
I must've screwed up; there's no way I could get that result with that DG'
Quaternary structure is associated with
the overall shape of the polypeptide chain
the sum of secondary and tertiary interactions
simple proteins with only one subunit
the relative orientation of one polypeptide to another polypeptide in a multi-subunit protein
Which of the following is not true concerning standard states?
For pure liquids, the standard state is 1M
For pure solids, the standard state is the pure solid itself
For gases, the standard state is 1 atmosphere
For solutes, the standard state is 1M
The main intracellular buffer system is
H3PO4/H2PO4-
H2PO4-/ HPO42-
HPO42-/PO43-
H3PO4/PO43-
Cellular metabolism-cellular chemical reactions that produce ATP to maintain homeostasis + cellular functions such as:
Cell growth and divison
Breakdown and replacement of components of a cell
Processes like secretion, contraction and propagation of action potentials
Body needs to build up energy reserves and store fuel as fat
All of these
Catabolism ______ and Anabolism ____
Is the breakdown or organic molecules in a series of steps to synthesize ATP or other high E compounds ; Synthesize new organic molecules
Synthesize new organic molecules ; Is the breakdown or organic molecules in a series of steps to synthesize ATP or other high E compounds
Entropy
The measure of a system's thermal energy per unit temperature that is unavailable for doing useful work. Because work is obtained from ordered molecular motion, the amount of entropy is also a measure of the molecular disorder, or randomness, of a system.
a thermodynamic quantity equivalent to the total heat content of a system. It is equal to the internal energy of the system plus the product of pressure and volume. The change in enthalpy associated with a particular chemical process. "Most compounds have negative enthalpies of formation"
Enthalpy
a thermodynamic quantity equivalent to the total heat content of a system. It is equal to the internal energy of the system plus the product of pressure and volume. The change in enthalpy associated with a particular chemical process. "Most compounds have negative enthalpies of formation"
The measure of a system's thermal energy per unit temperature that is unavailable for doing useful work. Because work is obtained from ordered molecular motion, the amount of entropy is also a measure of the molecular disorder, or randomness, of a system.
The disassociation of water
An equilibrium reaction in which one water molecule donates its proton to another water molecule. The water molecule that receives proton is acting as a base, and it converts to conjugate acid H3O+.
(also autoionization of water, and autodissociation of water) is an ionization reaction in pure water or in an aqueous solution, in which a water molecule, H2O, deprotonates (loses the nucleus of one of its hydrogen atoms) to become a hydroxide ion, OH−.
The Ionization of Water
An equilibrium reaction in which one water molecule donates its proton to another water molecule. The water molecule that receives proton is acting as a base, and it converts to conjugate acid H3O+.
(also autoionization of water, and autodissociation of water) is an ionization reaction in pure water or in an aqueous solution, in which a water molecule, H2O, deprotonates (loses the nucleus of one of its hydrogen atoms) to become a hydroxide ion, OH−.
Gibbs Free Energy (The energy to do work) (free energy)
The change in free energy (ΔG) is the difference between the heat released during a process and the heat released for the same process occurring in a reversible manner. If a system is at equilibrium, ΔG = 0
a high-energy state, and some amount of energy – the activation energy – must be added in order for the molecule reach it. Because the transition state is unstable, reactant molecules don't stay there long, but quickly proceed to the next step of the chemical reaction.
Transition state (high energy)
The change in free energy (ΔG) is the difference between the heat released during a process and the heat released for the same process occurring in a reversible manner. If a system is at equilibrium, ΔG = 0.
a high-energy state, and some amount of energy – the activation energy – must be added in order for the molecule reach it. Because the transition state is unstable, reactant molecules don't stay there long, but quickly proceed to the next step of the chemical reaction.
Difference in Gibbs free energy (G) and the transition state (high energy)
The transition state has the highest free energy, making it a rare and un-stable intermediate
The transition state has the lowest free energy state, making it rare and un-stable intermediate
An important part of the electron transport chain. They form an integral part of complex III, where they take up electrons from cytochrome c and pass them on to the copper ions and the bound oxygen in the cytochrome oxidase system.
Cytochromes A
Cytochromes B
Cytochromes C
Transport electrons from dehydrogenases to cytochrome c-type proteins or to iron–sulfur proteins.
Cytochromes A
Cytochromes B
Cytochromes C
Is primarily known for its function in the mitochondria as a key participant in the life-supporting function of ATP synthesis. However, when a cell receives an apoptotic stimulus, cytochrome c is released into the cytosol and triggers programmed cell death through apoptosis.
Cytochromes A
Cytochromes B
Cytochromes C
What is a heme?
An iron-containing cyclic compound found in cytochromes, hemoglobin, and myoglobin
Any of a group of hemoprotein cell components that, by readily undergoing reduction and oxidation (gain and loss of electrons) with the aid of enzymes, serve a vital function in the transfer of energy within cells. Hemoproteins are proteins linked to a nonprotein, iron-bearing component.
What is a cytochrome and its function?
Any of a group of hemoprotein cell components that, by readily undergoing reduction and oxidation (gain and loss of electrons) with the aid of enzymes, serve a vital function in the transfer of energy within cells. Hemoproteins are proteins linked to a nonprotein, iron-bearing component.
An iron-containing cyclic compound found in cytochromes, hemoglobin, and myoglobin
What is myoglobin and its function?
A protein that's found in your striated muscles, which includes skeletal muscles (the muscles attached to your bones and tendons) and heart muscles. Its main function is to supply oxygen to the cells in your muscles (myocytes)
A two-way respiratory carrier, transporting oxygen from the lungs to the tissues and facilitating the return transport of carbon dioxide.
what is a hemoglobin and its function?
A two-way respiratory carrier, transporting oxygen from the lungs to the tissues and facilitating the return transport of carbon dioxide.
A protein that's found in your striated muscles, which includes skeletal muscles (the muscles attached to your bones and tendons) and heart muscles. Its main function is to supply oxygen to the cells in your muscles (myocytes)
Coenzyme Q is also called
Ubiquinone or cytochrome c reductase
Hemoglobin
Myoglobin
cytochrome b
What is Chemosmotic coupling?
the mechanism for coupling electron transport to oxidative phosphorylation; it requires a proton gradient across the inner mitochondrial membrane
a series of reactions in the electron transport chain that provides the link between two electron transfers and one-electron transfers.
What is a Q cycle?
the mechanism for coupling electron transport to oxidative phosphorylation; it requires a proton gradient across the inner mitochondrial membrane
a series of reactions in the electron transport chain that provides the link between two electron transfers and one-electron transfers.
NADH-CoQ oxidoreductase, catalyzes the first steps of electron transport, namely the transfer of electrons from NADH to coenzyme Q (CoQ).
NADH-CoQ oxidoreductase, catalyzes the first steps of electron transport, namely the transfer of electrons from NADH to coenzyme Q (CoQ). This complex is an integral part of the inner mitochondrial membrane and includes, among other subunits, several proteins that contain an iron–sulfur cluster and the flavoprotein that oxidizes NADH
Complex I
Complex II
Complex III
Complex IV
What is another name for Complex II in the electron transport chain?
cytochrome c oxidase.
NADH-CoQ oxidoreductase.
cytochrome bc1 complex.
succinate-CoQ oxidoreductase.
Hydrophobic interactions may occur between the R groups of which of the following amino acids?
Tyr and Trp
Ser and Thr
Asp and Ala
Cys and Met
None of the above.
What is complex III also known as?
Cytochrome BC1 complex.
Cytochrome BC2 complex.
Cytochrome BC3 complex.
what is Complex I also known as?
Cytochrome BC1 complex.
NADH dehydrogenase/ NADH oxidoreductase
What amino acids can be hydrophilic that have hydrophilic interactions?
Serine.
Threonine.
Cysteine.
Asparagine.
Glutamine.
Tyrosine.
Serine.
Threonine.
Asparagine.
Glutamine.
Tyrosine.
Serine.
Threonine.
Cysteine.
Asparagine.
Glutamine.
None of these
Serine.
Threonine.
Cysteine.
Asparagine.
Tyrosine.
Why do people use creatine supplements?
They provide good short-termed energy
They provide muscle growth
They provide hydration
How do you activate a metabolic pathway?
You have to add ATP
You have to take away ATP
You have to add amino acids
You have to take away amino acids
What is a buffer?
solution usually containing an acid and a base
a salt, that tends to maintain a constant hydrogen ion concentration.
Both of these are correct
None of the above
THE LINKING OF AN EXERGONIC REACTION TO DRIVE AN ENDERGONIC REACTION IS CALLED:
COUPLING
A STATE FUNCTION
RESONANCE
CATABOLSIM
TRUE OR FALSE, VAN DER WAALS FORCES ARE VERY STRONGLY REPULSIVE AT SHORT NUCLEAR DISTANCES AND VERY WEAK AT LONG INTERNUCLEAR DISTANCES.
TRUE
FALSE
The enzyme lysozyme has an optimum pH close to 5. A suitable buffer would be?:
Acetate4.75
Ammonia9.25
Carbonic acid6.37, 10.20
Citric acid3.09, 4.75, 5.41
CONSIDER THE REACTION OF ALCOHOL DEHYDROGENASE.CH3−CH2OH + NAD+ → CH3−CHO + NADH + H+ETHANOL ACETALDEHYDE. WHICH IS THE OXIDIZING AGENT?
ETHANOL
NAD+
ACETALDEHYDE
NADH
H+
A SOLUTION WITH A [H+] CONCENTRATION OF 1 X 10-11 WOULD HAVE A PH VALUE OF ___ AND BE CONSIDERED A(N)?
PH = 11
PH = 12
PH = 7
PH = 5
THE FOLDED STATES OF GLOBULAR PROTEINS IN AQUEOUS SOLUTIONS ARESTABILIZED PRIMARILY BY ______.
HYDROPHOBIC INTERACTIONS
PEPTIDE BONDS
PHOSPHODIESTER BONDS
IONIC BONDS
DISULFIDE BONDS
WHAT TYPE OF BONDING INTERACTIONS OCCUR IN TERTIARY PROTEINS?
HYDROGEN BONDS
IONIC BONDS
HYDROPHOBIC INTERACTIONS
BONDING BETWEEN R GROUPS
ALL OF THE ABOVE
TRUE OR FALSE? IN CHEMISTRY, A “SALT BRIDGE “IS A COMBINATION OF TWO NON-COVALENT INTERACTIONS: HYDROGEN BONDING AND IONIC BONDING
TRUE
FALSE
THE STANDARD STATE OF A SOLUTION IS TAKEN AS
1 ATMOSPHERE OF PRESSURE.
THE PURE SOLUTE.
1 MOLAR CONCENTRATION.
NONE OF THE ABOVE
BIOCHEMISTS USE A MODIFIED VALUE FOR STANDARD VALUES BECAUSE?
THE PH IN LIVING SYSTEMS IS SELDOM, IF EVER, NEAR 0
THE PH IN LIVING SYSTEM STARTS AT 0.
THE PH IN A LIVING SYSTEM IS ALWAYS AROUND NEUTRAL, 7, PH
THE PH OF A 10^-8 M HCL SOLUTION PREPARED WITH PURE WATER AT PH 7.0 ISCLOSEST TO ____.
6.0
6.9
7.1
7.9
8.0
THE STANDARD STATE USUALLY USED IN BIOCHEMISTRY INCLUDES?
ALL CONCENTRATIONS AT 1M, EXCEPT FOR [H+], WHICH IS 1 X 10 -7 M
ALL CONCENTRATIONS AT 10M, EXCEPT FOR [H+], WHICH IS 1 X 10 -14 M
ALL CONCENTRATIONS AT 100M, EXCEPT FOR [H+], WHICH IS 1 X 10 -21 M
WHICH OF THE FOLLOWING STATEMENTS CONCERNING THE FREE ENERGY CHANGE IS FALSE?
THE ENERGY CHANGE FOR A REACTION DEPENDS ONLY ON THE INITIAL AND FINAL STATES, AND ISINDEPENDENT OF THE PATH TAKEN.
THE OVERALL ENERGY CHANGE FOR A REACTION COULD BE CALCULATED BY SUMMING THE ENERGY CHANGESFOR A SERIES OF SEPARATE REACTIONS THAT COULD CONVERT THE REACTANTS TO THE PRODUCTS.
THE RATE OF A REACTION CAN BE DETERMINED FROM THE ENERGY CHANGE.
THE ENERGY CHANGE IS A FUNCTION OF THE CONCENTRATIONS OF THE PRODUCTS AND REACTANTS AT START.
IN THE FINAL STEP OF GLYCOLYSIS ATP IS MADE THROUGH THE PROCESS OF:
SUBSTRATE LEVEL PHOSPHORYLATION
OXIDATIVE PHOSPHORYLATION
PHOTO-PHOSPHORYLATION
REDOX REACTIONS
NICOTINAMIDE ADENINE DINUCLEOTIDE IS A COENZYME IN MANY OXIDATION–REDUCTION REACTIONS. ITS STRUCTURE HAS THREE PARTS. WHAT ARE THEY?
A NICOTINAMIDE RING, AN ADENINE RING, AND TWO SUGAR–PHOSPHATE GROUPS LINKED TOGETHER.
A NICOTINAMIDE RING, AN ADENINE RING, AND THREE SUGAR–PHOSPHATE GROUPS LINKED TOGETHER.
A NICOTINAMIDE RING, AN ADENINE RING, AND TWO DINUCLEOTIDES
THE CONVERSION OF NAD+ TO NADH IS AN EXAMPLE OF REDUCTION BECAUSE
THE PYRIDINE RING LOSES ELECTRONS (AND A HYDROGEN)
THE PYRIDINE RING GAINS ELECTRONS (AND A HYDROGEN)
THE ADENINE RING LOSES ELECTRONS
THE ADENINE RING GAINS ELECTRONS
TRUE OR FALSE. HYDROGEN BONDING. HYDROGEN BONDING IS A SPECIAL TYPE OF INDUCED DIPOLE - INDUCED DIPOLE BOND
TRUE
FALSE
THE LOCATION OF PROSTHETIC GROUPS IS SHOWN IN THIS LEVEL OF STRUCTURE:
PRIMARY STRUCTURE
SECONDARY STRUCTURE
TIRTIARY STRUCTURE
QUATERNARY STRUCTURE
ALL OF THESE
WHAT TYPE OF BOND IS SHOWN INDICATED BY THE GREEN ARROW?
(S-S BOND IN PICTURE)
SALT BRIDGE
HYDROGEN
DISULFIDE
COMPLEX II OF THE ELECTRON TRANSPORT CHAIN OXIDIZES ____, REDUCES ____, AND ____ PROTONS IN THE PROCESS.
FADH2; COENZYME Q; PUMPS
NADH; COENZYME Q; DOESN'T PUMP
NADH; COENZYME Q; PUMPS
FADH2; COENZYME Q; DOESN'T PUMP
COMPLEX IV OF THE ELECTRON TRANSPORT CHAIN OXIDIZES ____, REDUCES ____, AND ____ PROTONS IN THE PROCESS.
COENZYME Q; CYTOCHROME C; PUMPS
CYTOCHROME C; COENZYME Q; PUMPS
CYTOCHROME C; O2; DOESN'T PUMP
CYTOCHROME C; O2; PUMPS
OF THE FOLLOWING SOLUTIONS, WHICH HAS THE GREATEST BUFFERING CAPACITY?
0.121 M HF AND 0.667 M NAF
0.821 M HF AND 0.909 M NAF
0.821 M HF AND 0.217 M NAF
0.100 M HF AND 0.217 M NAF
A BUFFER SOLUTION AT PH 10 HAS A RATIO OF [HA]/[A-] OF 10. WHAT IS THE PKA OF THE ACID?
8
9
10
11
12
CALCULATE THE FINAL PH OF A SOLUTION MADE BY THE ADDITION OF 10 ML OF A 0.5 M NAOH SOLUTION TO 500 ML OF A 0.4 M HA ORIGINALLY AT PH = 5.0 (PKA = 5.0) NEGLECT THE VOLUME CHANGE.
6.01
5.09
7.00
5.55
WHICH STATEMENTS APPLY TO ANABOLISM?
PROCEEDS IN STAGES
REQUIRES ENERGY
REQUIRES REDUCING AGENTS
ALL OF THE ABOVE
CONSIDER THIS RXN WHICH HAS A ΔG° = +0.4 KJ/MOL.A+B↔C+D, 1 M A, 1 M B, 0.1 M C AND 0.1 M D ARE ADDED TO A CONTAINER AT ROOM TEMPERATURE.WHAT CAN YOU SAY ABOUT THIS STATEMENT/REACTION THAT IS TRUE?
THE REACTION WILL PROCEED IN THE FORWARD DIRECTION TO REACH EQUILIBRIUM.
THE REACTION WILL RECEED IN THE BACKWARD DIRECTION TO REACH EQUILIBRIUM.
BY DEFINITION, A SPONTANEOUS REACTION IS ONE IN WHICH
ENERGY IS RELEASED. EXERGONIC.
ENERGY IS ABSORBED. EXERGONIC.
ENERGY IS RELEASED. ENDERGONIC
ENERGY IS ABSORBED ENDERGONIC.
THE BODY PERFORMS MANY PROCESSES THAT DEPEND UPON ENERGY AND COULD NOT OCCUR WITHOUT A SUPPLY OF ATP. HOW DOES THE ENERGY FROM ATP POWER THE CELLULAR REACTIONS?
THE CELLULAR PROCESSES ARE COUPLED TO HYDROLYSIS OF ATP, AN EXERGONIC PROCESS
CELLULAR PROCESSES ARE COUPLED TO HYDROLYSIS OF ATP, AN ENDERGONIC PROCESS
ENERGY FROM ATP HYDROLYSIS IS STORED IN CELLULAR CHAMBERS
ATP HYDROLYSIS ABSORBS THE REMAINING ENERGY FROM FORMATION OF GLUCOSE-6-PHOSPHATE
ALL OF THE ENERGY FROM HYDROLYSIS OF ATP IS RELEASED AS HEAT
SUPPOSE THAT YOU DETERMINED ΔG FOR A REACTION AT ROOM TEMPERATURE AND THEN CARRIED OUT THE SAME REACTION AT A HIGHER TEMPERATURE. AT HIGHER TEMPERATURES, ΔG FOR THE REACTION WILL BE:
A LARGER NEGATIVE NUMBER THAN AT ROOM TEMPERATURE
THE SAME AS AT ROOM TEMPERATURE
LOWER NEGATIVE NUMBER THAN AT ROOM TEMPERATURE
IMPOSSIBLE TO DETERMINE BECAUSE ΔG IS INDEPENDENT OF TEMPERATURE
ΔG FOR AN EXOTHERMIC REACTION IS:
>0
<0
=0
TRUE OR FALSE, BIOCHEMISTS/BIOLOGICAL CHEMISTS USE ΔG°′ WHERE THE PRIME SYMBOL (ΔG°′) INDICATES
TRUE
FALSE
THE PH OF A SOLUTION IS 10. WHAT IS ITS [H+] CONCENTRATION?
14
10
7
4
WHAT IS THE PH OF A SOLUTION FOR WHICH THE CONCENTRATION OF H+ IS 6.92×10−6 M ?
H+] = 10^-8.923 = 1.19X10^-9
H+] = 10^-8.943 = 1.19X10^-6
H+] = 10^-5.973 = 1.19X10^-7
H+] = 10^-8.623 = 1.19X10^-7
TRUE OR FALSE, THE Α HELIX, A COMMON STRUCTURAL MOTIF OF PROTEINS, CONSISTS OF A RIGHT-HANDED HELIX WITH A REPEAT LENGTH OF 3.6 AMINO ACID RESIDUES PER HELICAL TURN. THE Α HELIX IS STABILIZED BY HYDROGEN BONDS BETWEEN AN AMIDE HYDROGEN OF ONE AMINO ACID AND A CARBONYL OXYGEN FOUR AMINO ACIDS AWAY.
TRUE
FALSE
IN THE MALATE-ASPARTATE SHUTTLE, WHICH TWO SUBSTANCES CANNOT CROSS THE INNER MITOCHONDRIAL MEMBRANE DIRECTLY?
NADH AND OXALOACETATE
ASPARTATE AND MALATE
NAD+ AND PYRUVATE
NAD+ AND PYRUVATE
WHICH INTERMEDIATE OF THE CITRIC ACID OR TCA CYCLE IS ALSO INVOLVED IN THE MALATE-ASPARTATE SHUTTLE AND GLUCONEOGENESIS?
OXALOACETATE
MALATE
SUCCINYL-COA
ISOCITRATE
PROTEIN MISFOLDING IS BELIEVED TO BE THE PRIMARY CAUSE OF WHAT DISEASES?
ALZHEIMER'S DISEASE
PARKINSON'S DISEASE
HUNTINGTON'S DISEASE
ALL OF THE ABOVE
IN THE COENZYME FAD THE SITE TO WHICH ELECTRONS ARE TRANSFERRED IS
THE RIBOSE MOIETY OF THE MOLECULE
A PURINE RING SYSTEM
A PYRIMIDINE RING SYSTEM
A NITROGEN-CONTAINING RING SYSTEM
WHICH OF THE FOLLOWING GENE MUTATIONS IS LEAST LIKELY TO HAVE A HARMFUL EFFECT ON THE RESULTING PROTEIN?
MISSENSE
A FRAMESHIFT MUTATION
A NONSENSE MUTATION
THESE ARE ALL LIKELY TO HAVE A HARMFUL EFFECT ON THE RESULTING PROTEIN
WHAT HAPPENS TO THE ENTROPY OF A MOLECULE AS THE NUMBER OF RESONANCE STRUCTURES INCREASES?
ENTROPY ALSO INCREASES
ENTROPY DECREASES
ENTROPY HAS NO RELATIONSHIP TO THE NUMBER OF RESONANCE STRUCTURES
TRUE OR FALSE, NOT ALL ENERGETICALLY FAVORED REACTIONS ARE SPONTANEOUS. MANY TIMES SOME ENERGY OF ACTIVATION NEEDS TO BE ADDED. FOR EXAMPLE, PAPER (CELLULOSE = C6H12O6) EXISTS STABLY IN THE PRESENCE OF OXYGEN. EVEN THOUGH THE RAPID OXIDATION OF THE CELLULOSE TO FORM CO2, H2O AND C IS ENERGETICALLY FAVORED, THE PAPER WON'T BURN (BURNING = THE RAPID OXIDATION OF CELLULOSE) UNLESS ACTIVATION ENERGY (HEAT) IS APPLIED
TRUE
FALSE
AN HCL SOLUTION HAS A PH OF 3. IF YOU DILUTE 10 ML OF THE SOLUTION TO 1000ML, WHAT WILL THE FINAL PH BE?
PH = - LOG 0.00001 = 5
PH = - LOG 0.00001 = 7
PH = - LOG 0.00001 = 10
PH = - LOG 0.00001 = 3
