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MCAT Miscellaneous > Review 2 > Flashcards

Review 2 Flashcards

1
Q

Titration Indicators

A
  1. Methylated pH - 4.4-6.2 (~4-6)
  2. Bromothymol blue - 6.0-7.6 (~6-8)
  3. Phenolphthalein - 8.2-10 (~8-10)
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2
Q

Formula for pI

A

pI = (pKa1 + pKa2)/2

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3
Q

2 Ways to make a buffer

A
  1. Adding weak acid and weak base in equal amounts

2. Partially titrating weak acid with half strong base or partially titrating weak base with half strong acid

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4
Q

Bronsted-Lowry Acid and Base

A

BA - Proton donor

BB - Proton acceptor

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5
Q

Lewis Acid and Base

A

LA - Electron pair acceptor

LB - Electron pair donor

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6
Q

Amphoteric

A

Acid and Base consecutive properties

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7
Q

Amphipathic

A

Hydrophobic and hydrophilic properties

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8
Q

Strong Acids

A

HNO3, HCl, H2SO4, HI, HBr, and HClO4

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9
Q

Strong Bases

A

NaOH, KOH, Ca(OH)2, Mg(OH)2

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10
Q

Acidity with Ka and pKa

A

Lower the pKa, the higher the acidity. The higher the Ka, the higher the acidity

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11
Q

Basicity with Kb and pKb

A

Lower the pKb, the higher the basicity. The higher the Kb, the higher the basicity

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12
Q

Relationship between Ka and Kb

A

Ka*Kb = Kw

pKa + pKb = 14

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13
Q

Henderson-Hasselbach Equation

A

pH = pKa + Log[A-]/[HA]

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14
Q

Arrhenius Acid

A

Yields H3O+ when added to H2O

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15
Q

Arrhenius base

A

Yields OH- when added to H2O

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16
Q

Carboxylic acids/Carboxylates

A

RCOOH/RCOO-

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17
Q

Alkyl ammoniums/alkylamines

A

RNH3+/RNH2

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18
Q

Phenols/Phenoxides

A

C6H5OH/C6H5O-

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19
Q

Carbonic acid/Bicarbonate

A

H2CO3/HCO3-

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20
Q

Phosphoric acid/dihydrogen phosphate

A

HPO4/H2PO4

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21
Q

Non-metal hydroxides Type of Acid

A

Lewis Acids

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22
Q

Non-metal Oxides type of Acid

A

Bronsted-Lowry Acids

23
Q

Metal hydroxides Type of Base

A

Lewis Base

24
Q

Metal Oxides type of Base

A

Bronsted-Lowry Base

25
Q

Polyprotic Acids

A

The first proton is more acidic than the second one removed pKa1 < pKa2:
1. Carbonic acid (H2CO3)

  1. Sulfuric Acid (H2SO4)
  2. Phosphoric acid (H3PO4)
26
Q

Water and measurement of strong acid strength

A

Water cannot be used as a solvent since it goes to completion as it protonates fully from the strong acid

SOLUTION: Use a base weaker than the water as the standard solvent

27
Q

Water and measurement of weak acid strength

A

Weak acids are relatively stable because they do not easily deprotonate because it is their stable form.

SOLUTION: Water can be used here

28
Q

Halides and Electronegativity and Acidity

A

Halides size is not important. Electronegativity is more important

29
Q

RNA Virus Peculiarity

A
  1. They store genetic information as RNA
  2. They can replicate their RNA
  3. They can use their RNA as mRNA for translation
30
Q

Epigenetics and Method

A

Heritable changes in traits (DNA) without changing the sequence of DNA e.g:
1. DNA methylation

  1. Histone modification
31
Q

Another name of Peptide Bond

A

Nucleophilic addition-elimination Reaction

32
Q

Methods for breaking peptide bonds

A
  1. Acid hydrolysis (strong acids with heat)

2. Proteolysis (uses protease)

33
Q

Acid Hydrolysis vs. Proteolysis

A

Former is non-specific and latter is specific

34
Q

Peculiarity of Histidine, Proline, Glycine, and Cysteine

A

Histidine - pKa 6.5~7
Proline - R ring
Glycine - H instead of R and achiral
Cysteine - Can be reduced/oxidized (disulfide bonds)

35
Q

Cell and Redox Reactions

A

Extracellular = Oxidizing environment and Intracellular = Reducing environment

36
Q

Trick for Naming Land D of Amino acids with Fischer Projections

A

Look at the location of the amino group on the horizontal line

37
Q

Isoelectric point (pI) and Buffer

A
  • Point along the pH scale in which it exists in its neutral form
  • Personal thought is to use pI to predict the next pH change I think neutrality
38
Q

Factors on Protein Folding

A
  1. Temperature - (Destroys 2, 3, and 4) but not 1 (think of eggs
  2. pH - breaks ionic bonds
  3. Chemicals - break H-bonds
  4. Enzymes - Break covalent bonds (1)
39
Q

Folding Levels

A
  1. 1’ - Sequence (peptide bonds)
  2. 2’ - Backbone interactions (H-bonds)
  3. 3’ Distant interactions (VD, H, Hydrophobic, Disulfide bonds)
  4. 4’ - Subunit Same as 3’
40
Q

Ribose, Glucose, Fructose, Galactose, and Mannose Trick

A 
Ribose - All Right
Glucose - Left Fuck
Frustose - Ketose
Mannose - Left Gun
Galactose - C4 Epimer of glucose
41
Q

Lactose, Maltose, and Sucrose

A
  1. Lactose - Galactose and Glucose (Reducing sugar becasue of hemiacetal)
  2. Maltose - Glucose * 2 (Reducing sugar like lactose)
  3. Sucrose - Glucose and Fructose (Non-reducing sugar because of acetal)
42
Q

Branched Polysaccharide of Glucose

A

Glucose and Amylopectin

43
Q

How do the DNA strands know to orient themselves?

A
  1. -ve charges of Phosphate are moving away from each other (repulsion)
  2. N-bases want to be close because of H-bonds
44
Q

Methods of Enzyme Works

A
  1. Acid/Base Catalysis - H+
  2. Covalent modification - e-
  3. Electrostatic Catalysis - + and -
  4. Proximity and Orientation Effects
45
Q

Types of Enzymes

A
  1. Transferase
  2. Ligase
  3. Oxidoreductase
  4. Isomerase
  5. Hydrolase
  6. Lyase - Does not use redox or water to break bonds. Forms rings or double bonds
46
Q

Co-enzymes

A
  1. They are organic carrier molecules (NAD+, acetyl-coA)
47
Q

Co-factors

A

Help enzyme with catalysis and actually take part in catalysis e.g Magnesium with DNA (+ and -)

48
Q

Two particular environments that alter Enzyme function

A

pH and Temperature

49
Q

Assumptions made in Enzyme Kinetics

A
  1. Solutions are behaving ideally
    E + S ES E + P
  2. Constants are indeed constant
    [E] - Protein synthesis and degradation
    K - Environmental factors
  3. S -> P without enzyme is negligible
50
Q

Michaelis-Menton Equation

A

V0 = Vmax[S]/(Km+[S])

51
Q

V0

52
Q

Catalytic Efficiency

53
Q

Kcat

A

Turnover number - How many can it make into products in one sec

Vmax/Et

MCAT Miscellaneous (17 decks)

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