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Exercise Metabolism > Chapter Three: Proteins > Flashcards

Chapter Three: Proteins Flashcards

1
Q

What are amino acids?

A

The building blocks of proteins

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2
Q

What are the building blocks of proteins?

A

Amino acids

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3
Q

How many amino acids make up the proteins in our bodies?

A

20 amino acids

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4
Q

How many Amino Acids are essential?

A

Nine (9)

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5
Q

What does it mean for an amino acid to be “essential”?

A

It means that it can’t been synthesized by the body, it has to be consumed

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6
Q

What is the general formula for an Amino Acid?

A

Amino group

Central carbon (α) with side chain (R)

Carboxylic acid bound to next Amino Acid through an amide bond (peptide bond in proteins)

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7
Q

What determines a unique amino acid?

A

The side chain attached to the α-carbon

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8
Q

The side chain attached to the α-carbon determines:

A

Which unique amino acid it is

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9
Q

Which Amino Acids are positively charged?

A

Lysine
Arginine
Histidine

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10
Q

Which amino acids are negatively charged?

A

Aspartate
Glutamate

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11
Q

Which amino acids are polar?

A

Serine
Threonine
Asparagine
Glutamine

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12
Q

Which amino acids are special?

Which is the most important special amino acid?

A

Proline
Glycine
Cysteine

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13
Q

Which amino acids are hydrophobic?

A

Alanine
Valine
Leucine
Isoleucine
Phenylalanine
Tyrosine
Tryptophan
Methionine
Histadine

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14
Q

Two or more animo acids are linked together through:

A

Peptide bonds

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15
Q

Chains of amino acids linked together are known as:

A

Polypeptides

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16
Q

What is the primary structure of a polypeptide?

A

The sequence of amino acids, like a chain

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17
Q

What is the secondary structure in a polypeptide?

A

Local folding patterns like alpha helices and beta sheets

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18
Q

What is the tertiary structure of a polypeptide?

A

Completely folded, 3D shape of a long polypeptide chain

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19
Q

What is the quarternary structure of a polypeptide?

A

The arrangement of multiple polypeptide chains into a functional protein complex

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20
Q

The structure of a protein determines its:

A

Function

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21
Q

The function of a protein is determined by:

A

It’s structure

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22
Q

Slight changes into a proteins structure can be:

A

Transient and advantageous

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23
Q

Do slight changes to the structure of a protein denature a protein?

A

No

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24
Q

Big changes to the structure of a protein are:

A

Usually irreversible

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25
Q

Weak interactions that hold a protein in its tertiary structure can become disrupted. This is known as:

A

Denaturation

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26
Q

What can cause the denaturation of a protein?

A

High temp
Acidic/Alkaline changes
Ionic concentration (salting out)

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27
Q

What are prion diseases?

A

Disease that affect/prevent protein folding

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28
Q

What are chaperones?

A

Proteins that help proteins fold into their functional shapes

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29
Q

What helps proteins fold into their functional shapes?

A

Chaperones

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30
Q

Heat shock proteins are examples of:

A

Chaperones

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31
Q

What are catalytic proteins?

A

Enzymes

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32
Q

What class of proteins are enzymes?

A

Catalytic proteins

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33
Q

What proteins carry other substances?

A

Transport/Carrier proteins

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34
Q

What do transport/carrier proteins do?

A

Carry other substances

Like oxygen, fatty acids

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35
Q

Which proteins store cell components?

A

Storage proteins

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36
Q

What are motor proteins called?

A

Motile proteins

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37
Q

What do structure proteins do?

A

Provide mechanical support

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38
Q

What kind of proteins are antibodies?

A

Defensive proteins

39
Q

What do messenger proteins do?

A

Hormones and neurotransmitters

40
Q

What do receptors do?

A

Bind messenger proteins causing a response in a target cell

41
Q

What binds messenger proteins causing responses in target cells?

42
Q

What is the ultimate oxidant in the electron transport chain?

43
Q

What carries oxygen through biological fluids?

A

Carrier proteins

44
Q

What structure is hemoglobin?

A

Quaternary structure

45
Q

The most abundant protein in RBCs is:

A

Hemoglobin

46
Q

What group carries oxygen in the blood?

47
Q

Oxygen dissociates from hemoglobin in tissues because of:

A

The local decrease in oxygen pressure

48
Q

Hemoglobin can also carry:

A

CO2 and H+

CO is bad

49
Q

VO2max depends on:

A

Total amount of hemoglobin

50
Q

How does hemoglobin function?

A

Allostery (cooperativity)

51
Q

What is allostery?

A

Any bound O2 molecules favor the binding of additional O2 until hemoglobin is saturated

52
Q

Any bound O2 molecules favor the binding of additional O2 until hemoglobin is saturated. This is known as:

53
Q

What is loading?

A

When every O2 molecule binds more tightly than the last

54
Q

What is unloading?

A

Release of O2 occurs more readily as more O2 are removed

55
Q

Binding CO2, H+, or both favors:

A

the dissociation of O2, and vice versa

56
Q

What structure is myoglobin?

A

Tertiary structure

57
Q

What is located in muscle and receives O2 from the blood?

58
Q

Where is myoglobin located?

A

In the muscles

59
Q

What has higher affinity for oxygen than hemoglobin:

60
Q

How big is myoglobin compared to muscle fibers?

A

1/50th the size

61
Q

What prosthetic group is bound to a polypeptide that carries oxygen?

A

Heme group

62
Q

What does heme contain?

A

Fe2+ (Iron)

63
Q

What are enzymes?

A

Proteins, generally

64
Q

What is the function of an enzyme?

A

Accelerate biochemical reactions

65
Q

What functions as a biological catalyst?

66
Q

Are enzymes changes during a reaction?

67
Q

What are substrates?

A

The reactants of an enzymatic reaction

68
Q

The reactants of an enzymatic reaction are known as:

A

Substrates

69
Q

Substrates are converted to:

70
Q

How are enzymes named?

A

Usually named after their substrates

71
Q

Enzymes increase reaction velocities by:

A

10^5 to 10^17 times

Hundreds of thousands of reactions/second

72
Q

Enzymes can only act on specific substrates. This is known as:

A

High specificity

73
Q

The high specificity of enzymes means:

A

They only act on specific substrates

74
Q

The catalytic power of enzymes is highly:

75
Q

Because the catalytic power of enzymes is regulated, this gives organisms:

A

Great control over the rate of synthesis or breakdown of components

76
Q

Enzymes are very specific to their:

A

Substrates

77
Q

Enzymes react with their substrates at their:

A

Active sites

78
Q

Enzymes react with their substrates at their:

A

Active sites

79
Q

Enzymes react at their active sites with their:

A

Substrates

80
Q

The catalytic activity of enzymes occurs:

A

At the active site

81
Q

There are two models for substrate interaction. The Lock and Key Model, and the:

A

Induced Fit Model

82
Q

What is the induced fit model of substrate interaction?

A

When the active site doesn’t perfectly fit the substrate, and the interaction of the connection between the substrate and the active site modifies the shape of both

83
Q

Enzymes affect the rate of reaction. Not the:

A

Direction of reactions

84
Q

Rate of reaction =

A

The change in concentration of reactants or products of a reaction divided by time

85
Q

Enzyme activity is:

A

The catalytic power of the enzyme

86
Q

The catalytic power of the enzyme is indicated by an:

A

Increase in V

87
Q

What is ΔG++?

A

Free Energy of Activation

88
Q

Free Energy of Activation is always:

A

Positive, and lower with an enzyme

89
Q

What is the Free Energy of Activation?

A

The energy required to reach the transition state of a chemical reaction

90
Q

Can enzymes catalyze both directions of a reaction?

91
Q

Enzymes ___ catalyze both directions of a reaction.

92
Q

What are the five factors that affect the rate of enzyme reactions?

A

Substrate concentration
Enzyme concentration
Temp
pH
Ionic strength

93
Q

Substrate concentration
Enzyme concentration
Temp
pH
Ionic strength

These five factors:

A

Affect the rate of enzyme reactions

Exercise Metabolism (10 decks)

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