MCAT > Bio 1 > Flashcards

Bio 1 Flashcards

(93 cards)

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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
What are the 3 and 1 letter code for methionine?
met | M
26
What are the 3 and 1 letter code phenylalanine?
phe | F
27
What are the 3 and 1 letter code for proline?
pro | P
28
What are the 3 and 1 letter code for serine?
ser | S
29
What are the 3 and 1 letter code for threonine?
the | T
30
What are the 3 and 1 letter code for tryptophan?
trp | W
31
What are the 3 and 1 letter code for tyrosine?
tyr | Y
32
What are the 3 and 1 letter code for valine?
val | V
33
What are the two types of covalent bonds found in proteins?
peptide bonds | disulphide bonds
34
Which end of a protein is made first during synthesis?
amino terminus
35
Is protein hydrolysis thermodynamically favourable?
yes but it is kinetically slow
36
What is proteolysis/proteolytic cleavage?
hydrolysis of a protein by another protein
37
Which amino acid residue can form disulphide bonds? Which level of structure is this?
cysteine | tertiary structure
38
In what environment do disulphide bonds form?
oxidizing i.e. only in extracellular peptides
39
What are the 2 main secondary structure motifs?
alpha helix and beta pleated sheet
40
Describe an alpha helix
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
What makes sucrose?
glucose (alpha 1, 2) fructose
42
What make lactose?
galactose (beta 1,4) glucose
43
What makes maltose?
glucose (alpha 1, 4) glucose
44
What makes cellubiose?
glucose (beta 1,4) glucose
45
What makes glycogen?
glucose polymer with alpha 1,4 linkages and alpha 1, 6 branches
46
What is cellulose made of?
polymer of cellubiose (blu beta 1, 4 blu)
47
What is starch made of?
alpha 1,4 glucose polymer like glycogen, but the branching is a bit different
48
Is the hydrolysis of polysaccharides into monosaccharides favoured thermodynamically?
yes
49
What are the 3 physiological roles of lipids?
triglycerides store energy in adipoctyes phospholipids in cell membranes cholesterol has many roles including making steroid hormones
50
What configuration are naturally occurring double bonds in unsaturated fatty acids?
cis
51
What do fatty acids form in aqueous solutions?
micelles
52
What is saponification?
base-catalyzed hydrolysis of triglycerides into fatty acid salts (soaps)
53
What are lipases?
enzymes that hydrolyze fats
54
How does the oxidation/reduction of fats compare to that of carbs?
fats are much more reduced and thus store a lot more energy
55
What molecules make detergents?
phospholipids
56
How do phospholipids influence the fluidity of a membrane?
increasing unsaturation increases fluidity | increasing length decreases fluidity (i.e. shorter=more fluid)
57
How does cholesterol influence membrane fluidity?
at low temperatures it increases fluidity | at high temperatures it decreases fluidity
58
How many isoprene units are in a sesquiterpene?
3
59
Give an example of a terpenoid
vitamin A
60
What are steroids made of?
cholesterol
61
Is cholesterol amphipathic?
yes
62
What is pyrophosphate?
two phosphates bound via an anhydride linkage
63
What are the 3 reasons phosphate anhydride bonds store a lot of energy?
- 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
What is the first law of thermodynamics?
conservation of energy
65
What is delta G equal to?
delta G= delta H - TdeltaS
66
What do exergonic reactions have?
negative delta G
67
What do endergonic reactions have?
positive delta G
68
What do exothermic reactions have?
negative delta H
69
What do endothermic reactions have?
positive delta H
70
What does ln(1) equal?
0
71
Are free energy changes additive?
yes i.e. reaction coupling
72
Which conformation of sugars and amino acids do our bodies use?
L amino acids and D sugars
73
What are cofactors? Coenzymes?
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
Name 4 types of enzyme regulation. Are they all reversible?
``` covalent modification proteolytic cleavage association (w/other peptides) allosteric regulation They are all reversible except proteolytic cleavage ```
75
What is feedforward stimulation?
when an enzyme is stimulated by its substrate ( or a molecule used in the synthesis of its substrate)
76
Describe the relationship between Km and affinity of an enzyme for its substrate
low Km=high affinity
77
What kind of curve results from cooperative binding enzymes?
sigmoidal curve (S)
78
What is the relationship between cooperative and allosteric when referring to an enzyme?
cooperativity is a special type of allosteric interaction
79
Describe a competitive inhibitor and its effects
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
Describe a non-competitive inhibitor and its effects
``` 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
Describe an uncompetitive inhibitor and its effects
``` 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
Describe a mixed-type inhibitor and its effects
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
What are the 3 meanings of the word oxidize?
attach oxygen remove hydrogen remove electrons
84
What are the 3 meanings of the word reduce?
remove oxygen add hydrogen add electrons
85
Describe the regulation of hexokinase. What reaction does it catalyze?
catalyzes glucose to G6P activated by glucose inhibited by G6P
86
What is the committed step in glycolysis?
F6P to F16P
87
Describe the regulation of phosphofructokinase. What reaction does it catalyze?
catalyzes F6P to F16P inhibited by ATP activated by F2,6P and AMP
88
Describe the regulation of pyruvate kinase. What reaction does it catalyze?
catalyzes PEP to pyruvate activated by PEP and F16P inhibited by ATP
89
Describe the regulation of isocitrate dehydrogenase. What does it use and produce?
uses citrate, produces NADH and CO2 activated by ADP inhibited by ATP and NADH
90
What does the Kreb's cycle net per glucose molecule?
6 NADH 2 FADH2 4 CO2 2 GTP
91
How many protons and ATP do NADH and FADH2 net each in the electron transport chain/oxidative phosphorylation?
10 H+ / NADH = 2.5 ATP 6 H+/ FADH2 = 1.5 ATP 6 H+ / NADH from glycolysis = 1.5 ATP (4 H+ / ATP)
92
How many ATP are generated per glucose molecule in cell respiration?
30 ATP for eukaryotes | 32 ATP for prokaryotes
93
Describe the differences between prokaryotic and eukaryotic electron transport chain and oxidative phosphorylation
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

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