BIO Class 1 Flashcards

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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
Q

What is sucrose monosaccharides?

A

Glucose and fructose

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26
Q

What is lactose monosaccharides?

A

glucose and Galactose

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27
Q

What is the formula of maltose and why?

A

C12H22O11 because of dehydration synthesis

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28
Q

What is the animal glucose storage molecule?

A

Glycogen

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29
Q

What is the plant glucose storage molecule?

A

Starch

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30
Q

What is cellulose?

A

Plant structure

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31
Q

What are the three common polysaccharides?

A
  1. Glycogen
  2. Starch
  3. Cellulose
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32
Q

What is the main function of polysaccharides?

A

Energy

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33
Q

What are the main use of carbohydrates?

A

Energy and cell surface markers

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34
Q

What do unicellular can use carbs as?

A

Adhesion molecules

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35
Q

What is the monomer of lipids?

A

Hydrocarbons

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36
Q

What is saturated fatty acid?

A

No double bonds; solid

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37
Q

What is unsaturated fatty acid?

A

Kink in the chain; double bond

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38
Q

What is unsaturated at room temperature?

A

Liquid

39
Q

What is the structure of trans fat?

A

Have substituent on opposite sides of the double bond

40
Q

What is the problem with trans fat?

A

They can stack up on one another

41
Q

What is the most common way to find a fat?

A

Triglyceride

42
Q

What is the function of triglyceride?

A

Store energy

43
Q

What is the process of finding fatty acids in the body?

A

Esterification

44
Q

What is the phospholipid determined to be based on its properties?

A

Amphipathic; both polar and non polar

45
Q

What is terpene built from?

A

Isoprene units

46
Q

What is the propertiy of isoprene?

A

Hydrophobic

47
Q

What is the common function of squalene?

A

Waxes

48
Q

What is squalene?

A

6 isoprene together

49
Q

What is squalene a precursor to?

A

Ring lipids

50
Q

What is an example of a ring lipid?

A

Cholesterol

51
Q

What is the structure of steroid?

A

Cholesterol and derivatives (3 six carbon rings + 1 five carbon ring)

52
Q

What must be recognized for it to be cholesterol?

A

Ring structures

53
Q

What is the function of cholesterol?

A

Cell membrane, precursor to steroid hormones and bile salts

54
Q

What is the equation of thermodynamics?

A

∆G = ∆H - T∆S

55
Q

What are the variables in ∆G = ∆H - T∆S mean?

A

∆G: Gibbs free energy
∆H: Enthalpy
∆S: Kinetic energy

56
Q

What does it mean if ∆G is less than 0?

A

Spontaneous reaction

57
Q

What does it mean if ∆G is more than 0?

A

Nonspontaneous reaction

58
Q

What does it mean if ∆G is equal to 0?

A

Equilibrium

59
Q

What is exergonic reaction?

A

Energy released, ∆G is negative

60
Q

What is endergonic reaction?

A

Energy added, ∆G is positive

61
Q

What is the properties of transition state?

A

High energy and transient

62
Q

What is the reaction coordinate term?

A

x-axis in energy graph to show where you are in the reaction based one energy

63
Q

What do catalyst do?

A

Stabilize the transition state and reduce activation energy

64
Q

What are the 2 defining characteristics of enzymes?

A
  1. Increase rate of reaction
  2. Not be used up in reaction
  3. Specificity
65
Q

What is a major way of regulating enzymatic activity?

A

Phosphorylation

66
Q

What is a common way of regulating enzymatic activating involving another molecule?

A

Allosteric regulation

67
Q

What is a negative feedback loop?

A

The last element inhibits the first element

68
Q

What is a positive feedback loop?

A

Last element activates the first element

69
Q

What must positive feedback loop have?

A

Must have external regulator

70
Q

What is Vmax?

A

Rate of product formation at which the enzyme can catalyze

71
Q

What is Vmax dependent on?

A
  1. Enzyme concentration

2. Specific enzyme you are using

72
Q

What is Km in the V vs [S} graph?

A

[S} require dot reach half of Vmax like an affinity the E has for S

73
Q

The more affinity to the enzyme, how does that affect Km?

A

Km decreases

74
Q

What is a competitive inhibitor?

A

Bind to the active site

75
Q

How does active site effect Vmax and Km?

A

Vmax stays the same; Km increases

76
Q

What is non-competitive inhibition?

A

Allosteric regulation, turning enzyme off

77
Q

How does non-competitive effect Vmax and Km?

A

Vmax is lower, Km is unchanged

78
Q

What is uncompetitive inhibition?

A

Increases affinity to substrate but substrate stuck on enzyme

79
Q

Where does noncompetitive inhibition bind?

A

At allosteric site of enzyme along, does not change shape of active site

80
Q

Where does uncompetitive inhibition bind?

A

Binds allosteric site of ES complex

81
Q

What is the effect of uncompetitive inhibition on Vmax and Km?

A

Vmax decreased and Km decreased

82
Q

Where does a mixed inhibitor bind?

A

Binds to allosteric site alone and change active site or bind to ES complex

83
Q

What is the lineweaver-burk plot?

A

Inverse plot of 1/[V] and 1/[S}

84
Q

What happens when you move towards the origin on the inverse plot?

A

The denominator gets bigger

85
Q

What does the y-intercept represent in a LWB graph?

A

1/Vmax

86
Q

What does the x-intercept represent in a LWB graph?

A

-1/Km

87
Q

For a competitive inhibitor, what happens to the -1/m on inverse plot?

A

-1/km moves towards the right to be closer to the origin since it increases

88
Q

For a noncompetitive inhibitor, what happens to the 1/Vmax?

A

Decreases

89
Q

For a noncompetitive inhibitor, what happens to the 1/Vmax on inverse plot?

A

Would move upwards to get away from the origin since it decreases

90
Q

For a noncompetitive inhibitor, what happens to the -1/Km?

A

stays the same

91
Q

For a competitive inhibitor, what happens to the 1/Vmax on inverse plot?

A

Stays the same

92
Q

For a uncompetitive inhibitor, what happens to the 1/Vmax in the LWB plot?

A

Shift up to get away from the origin

93
Q

For a uncompetitive inhibitor, what happens to the -1/Km in the inverse plot?

A

shift to the left to get away from the origin

94
Q

Which reactions based on LWB plot are parallel?

A
  1. Uncompetitive and uninhibited

2. Noncomp and competitive