MCAT Biology 1: Molecules Flashcards

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1
Q

Major function of phospholipids:

A

Structural component of membranes

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2
Q

Major function of triacylglycerols [2]:

A
  1. Store metabolic energy

2. Thermal insulation and padding

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3
Q

Major function of steroids:

A

Metabolic activities

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4
Q

Major function of some fatty acids (eicosanoids):

A

Local hormones

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5
Q

These organs can absorb glucose in absence of insulin [2]:

A
  1. Brain (neural cells)

2. Liver (hepatic cells)

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6
Q

Parts/components of DNA [3]:

A
  1. Phosphate group
  2. 5-carbon sugar
  3. Nitrogenous base
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7
Q

Name the purines in DNA [2]:

A
  1. Adenine

2. Guanine

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8
Q

Name the pyrimidines in DNA [2]:

A
  1. Cytosine

2. Thymine

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9
Q

Number of H-bonds between GC [2]:

A

3

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10
Q

Number of H-bonds between AT [2]:

A

2

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11
Q

Number of rings in purines:

A

2

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12
Q

Number of rings in pyrimidines:

A

1

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13
Q

Protein 2° structure (alpha-helix/beta-sheet) reinforced by type of bond:

A

Hydrogen bond

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14
Q

Protein 2° structure (alpha-helix/beta-sheet) hydrogen bonds occur between:

A

Carbonyl oxygen – Hydrogen

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15
Q

Forces/bonds that contribute to 3° and 4° structure [5]:

A
  1. Covalent disulfide bonds
  2. Electrostatic (ionic) interactions
  3. Hydrogen bonds
  4. van der Waals forces
  5. Hydrophobic bonding
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16
Q

Amino acid causes kink in alpha-helix and beta-sheet and contributes to 3° structure:

A

Proline

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17
Q

Proline causes a kink by preventing type of bond:

A

Hydrogen bond

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18
Q

Factors that cause protein to lose higher-level conformation [3]:

A
  1. Heat
  2. Salt
  3. ∆pH
19
Q

Enzymes need these to function:

A

Cofactors

20
Q

Subcategories of cofactors [2]:

A
  1. Minerals

2. Coenzymes

21
Q

Many coenzymes come from:

A

Vitamins (or their derivatives)

22
Q

Competitive inhibitor binding site:

A

Enzyme active site

23
Q

Competitive inhibitor effect on Km:

A

Increase

24
Q

Competitive inhibitor effect of Vmax:

A

No change

25
Q

Uncompetitive inhibitor binding site:

A

E-S complex

26
Q

Uncompetitive inhibitor effect on Km:

A

Decrease

27
Q

Uncompetitive inhibitor effect on Vmax:

A

Decrease

28
Q

Mixed inhibitor binding site:

A

E-S complex or Enzyme

29
Q

Mixed inhibitor effect on Km:

A

Increase or Decrease

30
Q

Mixed inhibitor effect on Vmax:

A

Decrease

31
Q

Noncompetitive inhibitor binding site:

A

E-S complex or Enzyme

32
Q

Noncompetitive inhibitor effect on Km:

A

No change

33
Q

Noncompetitive inhibitor effect on Vmax:

A

Decrease

34
Q

Enzyme class catalyze transfer of electrons or hydrogen ions:

A

Oxidoreductases

35
Q

Enzyme class catalyze transfer of groups b/w locations:

A

Transferases

36
Q

Enzyme class regulate hydrolysis reactions:

A

Hydrolases

37
Q

Enzyme class catalyze reactions where functional groups added to double bond or vise versa:

A

Lyases

38
Q

Enzyme class catalyze transfer of groups within molecule:

A

Isomerases

39
Q

Enzyme class catalyze condensation reactions coupled to hydrolysis of high energy molecules:

A

Ligases

40
Q

Type of lyase that catalyzes addition of substrate to double bond of another:

A

Synthase

41
Q

Type of ligase that requires energy input from ATP or some other nucleotide:

A

Synthetase

42
Q

Enzyme type that phosphorylates:

A

Kinase

43
Q

Enzyme type that dephosphorylates:

A

Phosphatase