Biochemistry Final Review Flashcards

(50 cards)

1
Q

What is the primary purpose of a buffer in biochemistry?

A

To maintain a stable pH by resisting changes in H+ concentration.

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2
Q

How is ΔE° calculated using half-reactions?

A

ΔE° = E°(reduction half-reaction) - E°(oxidation half-reaction).

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3
Q

What does ΔG° represent in biochemical reactions?

A

The standard free energy change, indicating spontaneity of a reaction.

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4
Q

How do you calculate concentration after a dilution?

A

C1V1 = C2V2, where C is concentration and V is volume.

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5
Q

What determines the oxidation level of a compound?

A

The number of bonds to more electronegative atoms (e.g., O, N).

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6
Q

What is the expected charge of a small peptide at pH 7?

A

Depends on termini (NH3+ and COO-) and side chains (acidic/basic).

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7
Q

How are disulfide bonds formed in proteins?

A

Through oxidation of two cysteine thiol (-SH) groups.

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8
Q

What amino acids are typically found in the core of a protein?

A

Hydrophobic amino acids (e.g., Val, Leu, Ile).

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9
Q

What stabilizes an alpha helix in proteins?

A

Hydrogen bonds between backbone amides and carbonyls, and R-group interactions.

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10
Q

What is a reducing sugar?

A

A sugar with a free aldehyde or ketone group that can reduce other compounds.

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11
Q

How can you distinguish reducing from non-reducing sugars?

A

Reducing sugars have free aldehyde or ketone, 1–>4 bond.

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12
Q

What is the purpose of SDS-PAGE?

A

To separate proteins by molecular weight under denaturing conditions.

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13
Q

What type of DNA sequence do restriction enzymes recognize?

A

Palindromic sequences (e.g., GAATTC).

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14
Q

What does the hemoglobin-oxygen binding curve show?

A

Cooperative binding: R state (high affinity) and T state (low affinity).

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15
Q

What are the types of enzyme inhibitors?

A

Competitive, non-competitive, uncompetitive, and mixed inhibitors.

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16
Q

What stabilizes DNA structure in solution?

A

Hydrogen bonds, base stacking, and ionic interactions with cations.

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17
Q

What is catalytic efficiency (kcat/Km)?

A

A measure of how efficiently an enzyme converts substrate to product.

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18
Q

What is the role of glycosidic bonds in carbohydrates?

A

To link monosaccharides (e.g., α-1,4 in starch, β-1,4 in cellulose).

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19
Q

What are shared intermediates in the citric acid cycle and gluconeogenesis?

A

Oxaloacetate, citrate, and succinyl-CoA.

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20
Q

What is required for DNA synthesis primer?

A

A short single-stranded DNA or RNA sequence complementary to the template.

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21
Q

How are fatty acids named?

A

By carbon chain length and double bond positions (e.g., 18:1 Δ9).

22
Q

What factors influence membrane fluidity?

A

Fatty acid chain length, saturation (cis/trans), and cholesterol content.

23
Q

How does cis vs trans configuration affect melting point?

A

Cis fatty acids have lower melting points due to kinks in the chain.

24
Q

What are the products of fatty acid oxidation used for?

A

Energy (ATP), ketone bodies, and biosynthetic pathways.

25
What is secondary active transport?
Transport coupled to an ion gradient (e.g., Na+/glucose symport).
26
How is enzyme regulation influenced by ΔG°?
Reactions with large negative ΔG° are irreversible and tightly regulated.
27
What is the function of Complex I in the ETC?
Transfers electrons from NADH to ubiquinone, pumps protons.
28
How does dinitrophenol inhibit ATP synthesis?
It uncouples the ETC by dissipating the proton gradient.
29
Which amino acids are one-step converts to citric acid intermediates?
Glutamate → α-ketoglutarate, Aspartate → Oxaloacetate.
30
What is the key regulatory enzyme of glycolysis?
Phosphofructokinase-1 (PFK-1), inhibited by ATP and citrate.
31
What is the role of the pyruvate dehydrogenase complex?
Converts pyruvate to acetyl-CoA, linking glycolysis to the citric acid cycle.
32
What is the main product of the pentose phosphate pathway used for lipids?
NADPH, which provides reducing power for lipid biosynthesis.
33
What happens during β-oxidation of fatty acids?
Fatty acids are broken into acetyl-CoA units for energy production.
34
What determines lipoprotein density?
Higher protein content increases density (e.g., HDL > LDL).
35
What cofactor is used by aminotransferases?
Pyridoxal phosphate (PLP), derived from vitamin B6.
36
What is the end product of purine degradation in humans?
Uric acid.
37
How is urea synthesized in the urea cycle?
From ammonia, CO2, and aspartate, via ornithine and citrulline intermediates.
38
What is a conservative amino acid replacement?
Substitution with an amino acid of similar properties (e.g., Leu → Ile).
39
How are signals propagated along a neuronal axon?
Via action potentials driven by Na+ and K+ ion fluxes.
40
What are the fates of pyruvate?
Lactate, acetyl-CoA, oxaloacetate, alanine, or ethanol (varies by organism).
41
What activates a G-protein coupled receptor (GPCR)?
Ligand binding causes Gα subunit to exchange GDP for GTP and dissociate.
42
What is the structure of mature mRNA?
5' cap, coding exons, 3' poly-A tail; introns are removed.
43
How do you find the complementary DNA strand sequence?
A ↔ T, C ↔ G (e.g., 5'-ATCG-3' → 3'-TAGC-5').
44
What is the purpose of ELISA?
To detect and quantify proteins/antibodies using enzyme-linked antibodies.
45
How does fluorescence intensity change during protein unfolding?
Intensity decreases as temperature increases due to conformational changes.
46
What products are generated by photosystems?
ATP and NADPH (used in the Calvin cycle).
47
What is the principle of Sanger sequencing?
Uses dideoxynucleotides (ddNTPs) to terminate DNA synthesis at specific bases.
48
How is an open reading frame (ORF) identified?
Starts with a start codon (AUG) and ends with a stop codon (UAA, UAG, UGA).
49
What statistical test compares two-group data means?
A t-test determines if the difference is significant and accurate.
50
What does a confidence interval indicate?
The precision of a measurement; a narrower range is better.