Exam 3 Flashcards

1
Q

Which of the following is true about membrane proteins?

A

Lateral Diffusion occurs unless other cellular components restrict their movements.

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2
Q

Which of the following statements describe integral membrane proteins?

A

Amino Acids that contact the membrane are usually hydrophobic.

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3
Q

Which of the following is(are) not found as covalently attached anchors in lipid-linked proteins:

A

cholesterol and other sterols

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4
Q

Which of the following is not a general feature of the lipid bilayer in biological membranes?

A

They are all glycoproteins.

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5
Q

In humans, the fatty acid composition of membrane lipids in skin cells is different from the fatty acid composition of membrane lipids in the internal organs, because the internal organs function at a slightly higher temperature. which of the following differences in fatty acid composition is most likely to occur?

A

Skin cells show lower levels of 20:0 relative to 16:0 AND higher levels of 18:2 relative to 18:0.

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6
Q

Which of the following segments of the integral membrane protein glycophorin most likely contains the membrane-spanning sequence?

A

PEITLIIFGVMAGVIGTILL

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7
Q

Gap Junctions:

A

are important intercellular communication channels

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8
Q

Molecular Chaperones assist proteins in the formation of

A

tertiary structure

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9
Q

Oxygen triggers Hb to switch from its low affinity (T) state to its high affinity (R) state. What kind of allosteric effector is oxygen relative to Hb?

A

Homoallosteric; positive effector

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10
Q

The rearrangement of T-form hemoglobin to the R-form:

A

involves the movement of the Fe(II) into the heme plane.

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11
Q

Which of the following is NOT TRUE for the symmetry model of allosterism:

A

the ligand can bind to a subunit in either conformation

or

none of the above

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12
Q

One of the enzymes involved in glycolysis requires Zn2+ for catalysis. Under conditions of zinc deficiency, when the enzyme may lack zinc, the enzyme would be referred to as the ________.

A

apoenzyme

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13
Q

Which of the following statements is true of enzyme catalysts?

A

they bind to substrates, but are never covalently attached to substrate or product.

or

they lower activation energy for the conversion of substrate to product.

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14
Q

Using this reaction, the rate of breakdown of the enzyme-substrate complex (like any reaction rate) can be described by the expression ______________.

A

k-1[ES] + k2[ES]

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15
Q

To determine Km from a double reciprocal plot, you would _____.

A

multiply the reciprocal of the x-axis intercept by -1.

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16
Q

A metabolic pathway proceeds according to the scheme R -> S-> T-> U-> V-> W. A regulatory enzyme, X, catalyzes the first reaction pathway. Which of the following is most likely correct for this pathway?

A

The last product, W, is likely to be a negative modulator of X, leading to feedback inhibition.

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17
Q

What is the velocity of a first-order reaction when the reactant concentration is 6x10^-2 M and the rate constant is 8x10^3 sec^-1?

A

4.8 x 10^2 M*sec^-1

18
Q

Km is

A

the [S] that half-saturates the enzyme.

19
Q

Name a molecule that can be used to rearrange disulfide bonds within proteins and briefly describe how it works. (Beta-merchapthoethanol)

A

reducing agent that will cleave disulfide bonds and at low concentrations allows disulfides to reform (sometimes differently).

20
Q

Name a molecule that can be used to rearrange disulfide bonds within proteins and briefly describe how it works. PDI

A

protein disulfide isomerase - provides thiols that can replace thiols linked in another protein, which results in a shuffle or rearrangement of which thiols are covalently linked.

21
Q

What is the overall benefit of using cholesterol in membranes!

A

Cholesterol broadens the transition temperature range and at higher temps makes the membrane less fluid and at lower temps makes the membrane more fluid.

22
Q

Name two features of a membrane protein you would not see in cytoplasmic proteins.

A

transmembrane domain, signal sequence, asymmetric etc.

23
Q

Briefly describe the terminal end of a protein that has been prenylated.

A

The c-terminal end was cleaved (3 residues missing) to leave a c-terminal cys residue covalently linked to an isoprene group.

24
Q

T or F: Protein primary structures must be highly conserved to have the same active/binding site and function.

A

false

25
Q

List and briefly describe two methods that may be used to monitor protein folding events. CD

A

Circular Dichroism - spectroscopic method that monitors the optical rotation of the chiral carbons in the peptide backbone and indicates secondary structure.

26
Q

List and briefly describe two methods that may be used to monitor protein folding events. Pulsed H/D exchange

A

accessible hydrogens are exchanged for deuteriums and monitored via NMR.

27
Q

List and briefly describe two methods that may be used to monitor protein folding events. FRET

A

a fluorescence technique where energy is transferred from one fluorescent molecule (residue) to another only if they are in close proximity.

28
Q

Briefly describe how a protein can assist the folding of another protein folding.

A

proteins can provide an alternative environment (by binding or enclosing) for a portion of or a whole protein. This alternative environment typically stabilizes a portion (i.e. hydrophobic region) of the protein and allows additional folding pathways.

29
Q

Briefly describe the roles of clathrin, COPI, COPII proteins.

A

These proteins form cages around lipid vesicles to provide structural support. The various types (clathrin, COPI, COPII) are used in specific vesicle movement (i.e. clathrin from ER to plasma membrane, COPI from ER to golgi).

30
Q

Define the Levinthal Paradox.

A

Levinthal’s paradox is that finding the native folded state of a protein by a random search among all possible configurations can take an enormously long time.

31
Q

List the general steps in folding any protein.

A
  1. Secondary structure forms
  2. Hydrophobic collapse drives tertiary structure formation.
  3. Final tertiary interactions are formed.
32
Q

Describe one important weak interaction that plays a role in stabilizing the T or R state of Hemoglobin.

A

Electrostatic interactions between BPG and his residues in the central cavity that stabilize the T-state.

or

H-bonding between the alpha and beta subunits that stabilize the R-state.

33
Q

What types of interactions play a role between 3(CO2 and Hb) and 4(BPG and Hb)?

A

3: covalent bond when CO2 forms a carbamate with Hb
4: electrostatic interactions between BPG and positive His residues

34
Q

name a detergent used in biochemistry studies

A

SDS, Triton X-100, NP-40

35
Q

What are two general ways to control the level of enzyme activity present in an organism?

A
  1. Enzyme amount or level

2. Enzyme activity

36
Q

For the reaction shown above, what does the “steady state assumption” assume?

A

That the [ES] concentration is constant. The rate of ES breakdown equals the rate of formation.

37
Q

the enzyme efficiency of an enzyme, Ewild-type, was compared to a mutant version of the same enzyme Emutant… which form of the protein is most efficient for the substrate used?

A

The mutant enzyme is more efficient because the ratio of Kcat over Km is larger.

38
Q

Describe the interactions of a membrane protein with the rough ER during protein synthesis.

A

The membrane protein has a signal sequence. After this signal sequence is synthesized by the ribosome, it interacts with a protein that leads it to the ER where the signal sequence interacts with the translocon. The translocon spans the ER membrane and (1) provides a pore for the membrane to enter the ER and (2) inserts any membrane spanning regions into the ER membrane.

39
Q

Ligase

A

sticks two parts together

40
Q

Lyase

A

involves creating a double bond in carbon end product.

41
Q

Hydrolase

A

breaks apart parts and outputs water molecules