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Biochemistry > Class 3 E1 > Flashcards

Class 3 E1 Flashcards

1
Q

Increasing [S] decreases?

A

Keq

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2
Q

Increasing [P] increases?

A

Keq

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3
Q

The Keq is smaller when you have?

A

more reactants / substrates, higher denominator.

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4
Q

The Keq is larger when you have?

A

more product, higher numerator.

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5
Q

Equilibrium is not when?

A

S and P are equal.

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6
Q

ATP found at higher conc’s in cells vs. ADP. [ATP] >[ADP] when?

A

Coupled to another rxn.
Gradient of protons across mitochondrial membrane.
Produced through redox-rxns w/ enzymes that use a lot of E.

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7
Q 
Which of the following is a buffer system?
A. KCl and KOH
B. KCl and KNO3
C. HCl and NaOH
E.	H2O and HF
F.	H3PO4and H2PO3−
A

H3PO4 and H2PO3-

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8
Q

Why can’t a buffer system be made of HCl and NaOH?

A

they’re not conj. acid and base, both strong acids

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9
Q

AA’s make up

A

proteins.

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10
Q

What FG’s do all AA’s contain?

A

amine

carboxylic acid

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11
Q

All 22 AA residues differ in?

A

side chains.

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12
Q

AA aren’t available to H-bond because?

A

they’re bonded to the next AA in the peptide chain.

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13
Q

AA are usually what type of enantiomers?

A

L

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14
Q

AA’s are chiral except for?

A

glycine.

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15
Q

R – groups are

A

side chains and important FGs.

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16
Q

R – groups extend into which part of the enzyme?

A

binding pocket.

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17
Q

R – groups contribute to what type of interactions?

A

acid-base

protein-protein

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18
Q

R – groups form?

A

dimers.

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19
Q

Zwitterion

A

molecule w/ (-) and (+) charge.

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20
Q

AA at neutral pH is an example of a?

A

zwitterion.

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21
Q

AA ionized at a low pH (protonated, + charge) is an example of a?

A

zwitterion.

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22
Q

AA ionized at a high pH (deprotonated- charge) is an example of a?

A

zwitterion.

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23
Q

AA Classification:

Nonpolar (hydrophobic)

A

alkyl group
aromatic ring
H
fatty acid (hydrophobic and polar end)

24
Q

AA Classification:

Polar (hydrophilic)

A

acidic: carboxylate ion side chain.
basic: amino side chain
neutral: alcohol thiol, amide side chains.

25
Q

AA Classification:

Can AA’s be both polar and nonpolar?

A

yes, a little bit of each.

26
Q

The 7 AA’s with nonpolar side chains?

A 
Alanine
Valine
Leucine
Isoleucine
Methionine
Phenylalanine
Tryptophan
27
Q

The 2 AA’s with polar (-) charged side chains?

A

Aspartate

Glutamate

28
Q

The 3 AA’s with polar (+) charged side chains?

A

Lysine
Arginine
Histidine

29
Q

The 5 AA’s with polar uncharged side chains?

A 
Serine
Threonine
Glutamine
Asparagine
Tyrosine
30
Q

The 3 AA’s that have side chains with unique properties?

A

Glycine
Cysteine
Proline

31
Q

Properties of nonpolar side chains?

A

Hydrophobic
Incapable of H-bonding.
Aliphatic / aromatic.

32
Q

Properties of polar negatively charged side chains?

A

Contain a carboxyl group.

Commonly deprotonated at physiological pH.

33
Q

Properties of polar positively charged side chains?

A

Contain amino groups.

34
Q

Why are Lysine and Arginine positively charged at physiological pH?

A

Lysine (pKa 10.5)
Arginine (pKa 12.5)
They’re protonated at physiological pH.

35
Q

What happens to Histidine at physiological pH?

A

pKa of 6.0, partially protonated.

36
Q

Properties of polar uncharged side chains?

A

Hydrophilic

Not usually ionized at physiological pH.

37
Q

Glycine’s unique properties:

A

Fits into hydrophobic / hydrophilic environment.

Often resides at sites where 2 polypeptides are in close contact.

38
Q

Cysteine’s unique properties:

A

Able to form covalent bond w/ another cysteine to form a disulfide link.

39
Q

Proline’s unique properties:

A

Able to create kinks in polypeptide chains.

Can disrupt ordered secondary structure.

40
Q

AA side chains play a pivotal role in?

A

protein folding

protein-protein interaction

41
Q

Side chains can be ___ at diff pKa values?

A

ionized

42
Q

AA have an effect on the overall protein ___ and ___?

A

structure and function.

43
Q

How would the structure of Threonine be changed at a pH of 2 (acidic pH)

A

The carboxylic acid group would be protonated. (O-)

44
Q

Peptide Bond

A

linkage btw 2 AA’s, linear polymers of AA’s.

45
Q

How is a peptide bond formed?

A

an amide linkage btw the carboxyl of one AA and the amino of the next AA.

46
Q

Peptide bonds are what type of bond?

A

recurring.

47
Q

What is removed when a peptide bond is formed and what is the result of that?

A

a water molecule is removed, resulting in dehydration.

48
Q

What type of bond is a covalent linkage of trans configuration?

A

a peptide bond.

49
Q

Dipeptides

A

2 linked AA’s.

50
Q

Oligopeptides

A

4-20 AA’s.

51
Q

Polypeptides

A

20+ peptides linked together.

52
Q

Proteins tend to be more than how many AA’s?

A

100

53
Q

Monomers are single chains of AA folded into?

A

active protein.

54
Q

AA Modifications

A

Acetylation
Phosphorylation
Hydroxylation

55
Q

Acetylation

A

introduces an acetyl FG.

for a H atom

56
Q

Phosphorylation

A

rxn w/ a Pi or by transferring a phosphate from another Pi.

57
Q

Hydroxylation

A

introduces a hydroxyl into an ion or radical

usually by replacing a H atom

Biochemistry (10 decks)

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