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MCAT > Bio 1 > Flashcards

Bio 1 Flashcards

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MCAT flashcards
1
Q

Name the 9 non polar amino acids

A 
glycine
alanine
valine
methionine
leucine
isoleucine
proline
phenylalanine 
tryptophan
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2
Q

Name the 6 polar neutral amino acids

A 
serine
threonine
asparagine
glutamine
cysteine
tyrosine
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3
Q

Name the 2 polar acidic amino acids

A

aspartic acid

glutamic acid

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4
Q

Name the 3 polar basic amino acids

A

histidine
arginine
lysine

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5
Q

Are the polar neutral amino acids hydrophilic or hydrophobic?

A

hydrophilic

are polar enough to form H bonds with water

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6
Q

Which amino acids are usually phosphorylated by a kinase?

A

serine
threonine
tyrosine

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7
Q

What is the approximate pKa of the carboxylic acid functional group on the acidic amino acids?

A

~4

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8
Q

What is the approximate pKa for lysine?

A

~10

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9
Q

What is the approximate pKa for arginine?

A

~12

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10
Q

What is the approximate pKa for histidine?

A

~6.5

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11
Q

What is unique about histidine?

A

its side chain pKa is close to neutral so it can be protonated or unprotonated at physiological pH and thus often acts as a proton acceptor and donor

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12
Q

What are the 8 essential amino acids?

A 
valine
leucine
isoleucine 
phenylalanine 
tryptophan 
methionine 
threonine 
lysine
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13
Q

What are the 3 and 1 letter code for alanine?

A

ala

A

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14
Q

What are the 3 and 1 letter code for arginine?

A

arg

R

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15
Q

What are the 3 and 1 letter code for asparagine?

A

asn

N

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16
Q

What are the 3 and 1 letter code for aspartic acid?

A

asp

D

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17
Q

What are the 3 and 1 letter code for cysteine?

A

cys

C

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18
Q

What are the 3 and 1 letter code of glutamic acid?

A

glu

E

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19
Q

What are the 3 and 1 letter code of glutamine?

A

gln

Q

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20
Q

What are the 3 and 1 letter code of glycine?

A

gly

G

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21
Q

What are the 3 and one letter code for histidine?

A

his

H

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22
Q

What are the 3 and 1 letter code for isoleucine?

A

ile

I

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23
Q

What are the 3 and 1 letter code for leucine?

A

leu

L

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24
Q

What are the 3 and 1 letter code for lysine?

A

lys

K

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25
Q

What are the 3 and 1 letter code for methionine?

A

met

M

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26
Q

What are the 3 and 1 letter code phenylalanine?

A

phe

F

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27
Q

What are the 3 and 1 letter code for proline?

A

pro

P

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28
Q

What are the 3 and 1 letter code for serine?

A

ser

S

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29
Q

What are the 3 and 1 letter code for threonine?

A

the

T

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30
Q

What are the 3 and 1 letter code for tryptophan?

A

trp

W

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31
Q

What are the 3 and 1 letter code for tyrosine?

A

tyr

Y

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32
Q

What are the 3 and 1 letter code for valine?

A

val

V

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33
Q

What are the two types of covalent bonds found in proteins?

A

peptide bonds

disulphide bonds

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34
Q

Which end of a protein is made first during synthesis?

A

amino terminus

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35
Q

Is protein hydrolysis thermodynamically favourable?

A

yes but it is kinetically slow

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36
Q

What is proteolysis/proteolytic cleavage?

A

hydrolysis of a protein by another protein

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37
Q

Which amino acid residue can form disulphide bonds? Which level of structure is this?

A

cysteine

tertiary structure

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38
Q

In what environment do disulphide bonds form?

A

oxidizing i.e. only in extracellular peptides

39
Q

What are the 2 main secondary structure motifs?

A

alpha helix and beta pleated sheet

40
Q

Describe an alpha helix

A

always right-handed
5 angstroms in width
each sub sequent AA rising 1.5 angstroms
alpha carboxyl oxygen of one AA H-bonded to the alpha amino proton of another AA 3 residues away

41
Q

What makes sucrose?

A

glucose (alpha 1, 2) fructose

42
Q

What make lactose?

A

galactose (beta 1,4) glucose

43
Q

What makes maltose?

A

glucose (alpha 1, 4) glucose

44
Q

What makes cellubiose?

A

glucose (beta 1,4) glucose

45
Q

What makes glycogen?

A

glucose polymer with alpha 1,4 linkages and alpha 1, 6 branches

46
Q

What is cellulose made of?

A

polymer of cellubiose (blu beta 1, 4 blu)

47
Q

What is starch made of?

A

alpha 1,4 glucose polymer like glycogen, but the branching is a bit different

48
Q

Is the hydrolysis of polysaccharides into monosaccharides favoured thermodynamically?

A

yes

49
Q

What are the 3 physiological roles of lipids?

A

triglycerides store energy in adipoctyes
phospholipids in cell membranes
cholesterol has many roles including making steroid hormones

50
Q

What configuration are naturally occurring double bonds in unsaturated fatty acids?

A

cis

51
Q

What do fatty acids form in aqueous solutions?

A

micelles

52
Q

What is saponification?

A

base-catalyzed hydrolysis of triglycerides into fatty acid salts (soaps)

53
Q

What are lipases?

A

enzymes that hydrolyze fats

54
Q

How does the oxidation/reduction of fats compare to that of carbs?

A

fats are much more reduced and thus store a lot more energy

55
Q

What molecules make detergents?

A

phospholipids

56
Q

How do phospholipids influence the fluidity of a membrane?

A

increasing unsaturation increases fluidity

increasing length decreases fluidity (i.e. shorter=more fluid)

57
Q

How does cholesterol influence membrane fluidity?

A

at low temperatures it increases fluidity

at high temperatures it decreases fluidity

58
Q

How many isoprene units are in a sesquiterpene?

A

3

59
Q

Give an example of a terpenoid

A

vitamin A

60
Q

What are steroids made of?

A

cholesterol

61
Q

Is cholesterol amphipathic?

A

yes

62
Q

What is pyrophosphate?

A

two phosphates bound via an anhydride linkage

63
Q

What are the 3 reasons phosphate anhydride bonds store a lot of energy?

A
  • when bound together their negative charges repel each other
  • orthophosphate (one by itself) has more resonance forms than when linked
  • orthophosphate has a more favourable interaction with water than linked phosphates
64
Q

What is the first law of thermodynamics?

A

conservation of energy

65
Q

What is delta G equal to?

A

delta G= delta H - TdeltaS

66
Q

What do exergonic reactions have?

A

negative delta G

67
Q

What do endergonic reactions have?

A

positive delta G

68
Q

What do exothermic reactions have?

A

negative delta H

69
Q

What do endothermic reactions have?

A

positive delta H

70
Q

What does ln(1) equal?

A

0

71
Q

Are free energy changes additive?

A

yes i.e. reaction coupling

72
Q

Which conformation of sugars and amino acids do our bodies use?

A

L amino acids and D sugars

73
Q

What are cofactors? Coenzymes?

A

cofactors are metal ions or small molecules that aren’t themselves proteins that are required for activity in many enzymes
coenzymes are cofactors that are organic molecules

74
Q

Name 4 types of enzyme regulation. Are they all reversible?

A 
covalent modification 
proteolytic cleavage 
association (w/other peptides)
allosteric regulation
They are all reversible except proteolytic cleavage
75
Q

What is feedforward stimulation?

A

when an enzyme is stimulated by its substrate ( or a molecule used in the synthesis of its substrate)

76
Q

Describe the relationship between Km and affinity of an enzyme for its substrate

A

low Km=high affinity

77
Q

What kind of curve results from cooperative binding enzymes?

A

sigmoidal curve (S)

78
Q

What is the relationship between cooperative and allosteric when referring to an enzyme?

A

cooperativity is a special type of allosteric interaction

79
Q

Describe a competitive inhibitor and its effects

A

binds to the active site (often resembles transition state)
competes with substrate
doesn’t change Vmax
increases Km
(can be overcome by adding enough substrate)

80
Q

Describe a non-competitive inhibitor and its effects

A 
binds to an allosteric site 
decreases enzyme activity 
decreases Vmax
doesn't change Km 
(substrate can still bind to enzyme, there just isn't any catalytic activity)
81
Q

Describe an uncompetitive inhibitor and its effects

A 
binds to the enzyme-substrate complex
decreases enzyme activity 
decreases Vmax 
decreases Km 
(enzyme and substrate cannot dissociate thus it is increases the affinity)
82
Q

Describe a mixed-type inhibitor and its effects

A

binds to the enzyme or the enzyme-substrate complex
decreases Vmax
effects of Km depend:
if inhibitor has a greater affinity for the E-S complex then Km decreases
if inhibitor has a greater affinity for the E then Km increases
if inhibitor has equal affinity for E-S and E then Km doesn’t change

83
Q

What are the 3 meanings of the word oxidize?

A

attach oxygen
remove hydrogen
remove electrons

84
Q

What are the 3 meanings of the word reduce?

A

remove oxygen
add hydrogen
add electrons

85
Q

Describe the regulation of hexokinase. What reaction does it catalyze?

A

catalyzes glucose to G6P
activated by glucose
inhibited by G6P

86
Q

What is the committed step in glycolysis?

A

F6P to F16P

87
Q

Describe the regulation of phosphofructokinase. What reaction does it catalyze?

A

catalyzes F6P to F16P
inhibited by ATP
activated by F2,6P and AMP

88
Q

Describe the regulation of pyruvate kinase. What reaction does it catalyze?

A

catalyzes PEP to pyruvate
activated by PEP and F16P
inhibited by ATP

89
Q

Describe the regulation of isocitrate dehydrogenase. What does it use and produce?

A

uses citrate, produces NADH and CO2
activated by ADP
inhibited by ATP and NADH

90
Q

What does the Kreb’s cycle net per glucose molecule?

A

6 NADH
2 FADH2
4 CO2
2 GTP

91
Q

How many protons and ATP do NADH and FADH2 net each in the electron transport chain/oxidative phosphorylation?

A

10 H+ / NADH = 2.5 ATP
6 H+/ FADH2 = 1.5 ATP
6 H+ / NADH from glycolysis = 1.5 ATP
(4 H+ / ATP)

92
Q

How many ATP are generated per glucose molecule in cell respiration?

A

30 ATP for eukaryotes

32 ATP for prokaryotes

93
Q

Describe the differences between prokaryotic and eukaryotic electron transport chain and oxidative phosphorylation

A

prokaryotes don’t have membrane-bound organelles so their ETC is in the cell membrane
prokaryotes H+ are pumps from cytoplasm to extracellular and then come back in through ATP synthase (eukaryotes pumped to inter membrane space and the come back across the IMM to matrix)
prokaryotes net 32 ATP/glucose
eukaryotes net 30 ATP/glucose

MCAT (15 decks)

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