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MCAT BIOLOGY FLASHCARDS > BIO Class 1 > Flashcards

BIO Class 1 Flashcards

1
Q

What are polymers?

A

Macromolecules made from monomers

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2
Q

What is polymerization?

A

Reactions between these macromolecules

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3
Q

What is condensation?

A

Bind a molecule with water

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4
Q

What is hydrolysis?

A

Split a molecule with water

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5
Q

What is the monomer for proteins?

A

Amino acids

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6
Q

What is the structure of an amino acid?

A

Amine, side chain and carboxylic acid

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7
Q

What are the classifications of amino acids?

A

Polar, non polar, acidic, basic and neutral

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8
Q

What binds amino acids together?

A

Peptide bond

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9
Q

What is the direction of the synthesis of the amino acids?

A

N -> C synthesis

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10
Q

What is the primary structure of protein?

A

Amino acid sequence

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11
Q

What is the secondary structure of protein?

A

Hydrogen bonding between backbone atoms

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12
Q

What are the two types of secondary structure?

A

Alpha-helix and beta-pleated sheets

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13
Q

What is tertiary structure?

A

Folding due to side chain interactions with a polypeptide

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14
Q

What are the two main types of tertiary structure interactions?

A

Non-covalent and covalent

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15
Q

What are the three types of non-covalent bonding between protein structure?

A
  1. non polar / nonpolar
  2. polar neutral / polar neutral
  3. acid / base (electrostatic)
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16
Q

What are the covalent bondings between protein structures?

A

Disulfide bridges

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17
Q

What is quaternary structure?

A

Side chain interactions between different polypeptides

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18
Q

What is the monomer of carbohydrates?

A

Monosaccharides

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19
Q

What is the equation for monosaccharides?

A

CnH2nOn

1:2:1 ratio

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20
Q

What are the three common monosaccharides?

A
  1. Glucose
  2. Fructose
  3. Galactose
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21
Q

What is the similarity between glucose, fructose and galactose?

A

They all have the same formula, C6H12O6

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22
Q

What are the 5 carbon sugars?

A

Ribose and deoxyribose

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23
Q

What are the 3 common disaccharides?

A
  1. Maltose
  2. Sucrose
  3. Lactose
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24
Q

What is maltose monosaccharides?

A

Glucose and glucose

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25
What is sucrose monosaccharides?
Glucose and fructose
26
What is lactose monosaccharides?
glucose and Galactose
27
What is the formula of maltose and why?
C12H22O11 because of dehydration synthesis
28
What is the animal glucose storage molecule?
Glycogen
29
What is the plant glucose storage molecule?
Starch
30
What is cellulose?
Plant structure
31
What are the three common polysaccharides?
1. Glycogen 2. Starch 3. Cellulose
32
What is the main function of polysaccharides?
Energy
33
What are the main use of carbohydrates?
Energy and cell surface markers
34
What do unicellular can use carbs as?
Adhesion molecules
35
What is the monomer of lipids?
Hydrocarbons
36
What is saturated fatty acid?
No double bonds; solid
37
What is unsaturated fatty acid?
Kink in the chain; double bond
38
What is unsaturated at room temperature?
Liquid
39
What is the structure of trans fat?
Have substituent on opposite sides of the double bond
40
What is the problem with trans fat?
They can stack up on one another
41
What is the most common way to find a fat?
Triglyceride
42
What is the function of triglyceride?
Store energy
43
What is the process of finding fatty acids in the body?
Esterification
44
What is the phospholipid determined to be based on its properties?
Amphipathic; both polar and non polar
45
What is terpene built from?
Isoprene units
46
What is the propertiy of isoprene?
Hydrophobic
47
What is the common function of squalene?
Waxes
48
What is squalene?
6 isoprene together
49
What is squalene a precursor to?
Ring lipids
50
What is an example of a ring lipid?
Cholesterol
51
What is the structure of steroid?
Cholesterol and derivatives (3 six carbon rings + 1 five carbon ring)
52
What must be recognized for it to be cholesterol?
Ring structures
53
What is the function of cholesterol?
Cell membrane, precursor to steroid hormones and bile salts
54
What is the equation of thermodynamics?
∆G = ∆H - T∆S
55
What are the variables in ∆G = ∆H - T∆S mean?
∆G: Gibbs free energy ∆H: Enthalpy ∆S: Kinetic energy
56
What does it mean if ∆G is less than 0?
Spontaneous reaction
57
What does it mean if ∆G is more than 0?
Nonspontaneous reaction
58
What does it mean if ∆G is equal to 0?
Equilibrium
59
What is exergonic reaction?
Energy released, ∆G is negative
60
What is endergonic reaction?
Energy added, ∆G is positive
61
What is the properties of transition state?
High energy and transient
62
What is the reaction coordinate term?
x-axis in energy graph to show where you are in the reaction based one energy
63
What do catalyst do?
Stabilize the transition state and reduce activation energy
64
What are the 2 defining characteristics of enzymes?
1. Increase rate of reaction 2. Not be used up in reaction 3. Specificity
65
What is a major way of regulating enzymatic activity?
Phosphorylation
66
What is a common way of regulating enzymatic activating involving another molecule?
Allosteric regulation
67
What is a negative feedback loop?
The last element inhibits the first element
68
What is a positive feedback loop?
Last element activates the first element
69
What must positive feedback loop have?
Must have external regulator
70
What is Vmax?
Rate of product formation at which the enzyme can catalyze
71
What is Vmax dependent on?
1. Enzyme concentration | 2. Specific enzyme you are using
72
What is Km in the V vs [S} graph?
[S} require dot reach half of Vmax like an affinity the E has for S
73
The more affinity to the enzyme, how does that affect Km?
Km decreases
74
What is a competitive inhibitor?
Bind to the active site
75
How does active site effect Vmax and Km?
Vmax stays the same; Km increases
76
What is non-competitive inhibition?
Allosteric regulation, turning enzyme off
77
How does non-competitive effect Vmax and Km?
Vmax is lower, Km is unchanged
78
What is uncompetitive inhibition?
Increases affinity to substrate but substrate stuck on enzyme
79
Where does noncompetitive inhibition bind?
At allosteric site of enzyme along, does not change shape of active site
80
Where does uncompetitive inhibition bind?
Binds allosteric site of ES complex
81
What is the effect of uncompetitive inhibition on Vmax and Km?
Vmax decreased and Km decreased
82
Where does a mixed inhibitor bind?
Binds to allosteric site alone and change active site or bind to ES complex
83
What is the lineweaver-burk plot?
Inverse plot of 1/[V] and 1/[S}
84
What happens when you move towards the origin on the inverse plot?
The denominator gets bigger
85
What does the y-intercept represent in a LWB graph?
1/Vmax
86
What does the x-intercept represent in a LWB graph?
-1/Km
87
For a competitive inhibitor, what happens to the -1/m on inverse plot?
-1/km moves towards the right to be closer to the origin since it increases
88
For a noncompetitive inhibitor, what happens to the 1/Vmax?
Decreases
89
For a noncompetitive inhibitor, what happens to the 1/Vmax on inverse plot?
Would move upwards to get away from the origin since it decreases
90
For a noncompetitive inhibitor, what happens to the -1/Km?
stays the same
91
For a competitive inhibitor, what happens to the 1/Vmax on inverse plot?
Stays the same
92
For a uncompetitive inhibitor, what happens to the 1/Vmax in the LWB plot?
Shift up to get away from the origin
93
For a uncompetitive inhibitor, what happens to the -1/Km in the inverse plot?
shift to the left to get away from the origin
94
Which reactions based on LWB plot are parallel?
1. Uncompetitive and uninhibited | 2. Noncomp and competitive

MCAT BIOLOGY FLASHCARDS (23 decks)

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