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Exercise Metabolism > Chapter Three: Proteins > Flashcards

Chapter Three: Proteins Flashcards

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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
Weak interactions that hold a protein in its tertiary structure can become disrupted. This is known as:
Denaturation
26
What can cause the denaturation of a protein?
High temp Acidic/Alkaline changes Ionic concentration (salting out)
27
What are prion diseases?
Disease that affect/prevent protein folding
28
What are chaperones?
Proteins that help proteins fold into their functional shapes
29
What helps proteins fold into their functional shapes?
Chaperones
30
Heat shock proteins are examples of:
Chaperones
31
What are catalytic proteins?
Enzymes
32
What class of proteins are enzymes?
Catalytic proteins
33
What proteins carry other substances?
Transport/Carrier proteins
34
What do transport/carrier proteins do?
Carry other substances Like oxygen, fatty acids
35
Which proteins store cell components?
Storage proteins
36
What are motor proteins called?
Motile proteins
37
What do structure proteins do?
Provide mechanical support
38
What kind of proteins are antibodies?
Defensive proteins
39
What do messenger proteins do?
Hormones and neurotransmitters
40
What do receptors do?
Bind messenger proteins causing a response in a target cell
41
What binds messenger proteins causing responses in target cells?
Receptors
42
What is the ultimate oxidant in the electron transport chain?
Oxygen
43
What carries oxygen through biological fluids?
Carrier proteins
44
What structure is hemoglobin?
Quaternary structure
45
The most abundant protein in RBCs is:
Hemoglobin
46
What group carries oxygen in the blood?
Heme
47
Oxygen dissociates from hemoglobin in tissues because of:
The local decrease in oxygen pressure
48
Hemoglobin can also carry:
CO2 and H+ CO is bad
49
VO2max depends on:
Total amount of hemoglobin
50
How does hemoglobin function?
Allostery (cooperativity)
51
What is allostery?
Any bound O2 molecules favor the binding of additional O2 until hemoglobin is saturated
52
Any bound O2 molecules favor the binding of additional O2 until hemoglobin is saturated. This is known as:
Allostery
53
What is loading?
When every O2 molecule binds more tightly than the last
54
What is unloading?
Release of O2 occurs more readily as more O2 are removed
55
Binding CO2, H+, or both favors:
the dissociation of O2, and vice versa
56
What structure is myoglobin?
Tertiary structure
57
What is located in muscle and receives O2 from the blood?
Myoglobin
58
Where is myoglobin located?
In the muscles
59
What has higher affinity for oxygen than hemoglobin:
Myoglobin
60
How big is myoglobin compared to muscle fibers?
1/50th the size
61
What prosthetic group is bound to a polypeptide that carries oxygen?
Heme group
62
What does heme contain?
Fe2+ (Iron)
63
What are enzymes?
Proteins, generally
64
What is the function of an enzyme?
Accelerate biochemical reactions
65
What functions as a biological catalyst?
Enzymes
66
Are enzymes changes during a reaction?
No
67
What are substrates?
The reactants of an enzymatic reaction
68
The reactants of an enzymatic reaction are known as:
Substrates
69
Substrates are converted to:
Products
70
How are enzymes named?
Usually named after their substrates
71
Enzymes increase reaction velocities by:
10^5 to 10^17 times Hundreds of thousands of reactions/second
72
Enzymes can only act on specific substrates. This is known as:
High specificity
73
The high specificity of enzymes means:
They only act on specific substrates
74
The catalytic power of enzymes is highly:
Regulated
75
Because the catalytic power of enzymes is regulated, this gives organisms:
Great control over the rate of synthesis or breakdown of components
76
Enzymes are very specific to their:
Substrates
77
Enzymes react with their substrates at their:
Active sites
78
Enzymes react with their substrates at their:
Active sites
79
Enzymes react at their active sites with their:
Substrates
80
The catalytic activity of enzymes occurs:
At the active site
81
There are two models for substrate interaction. The Lock and Key Model, and the:
Induced Fit Model
82
What is the induced fit model of substrate interaction?
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
Enzymes affect the rate of reaction. Not the:
Direction of reactions
84
Rate of reaction =
The change in concentration of reactants or products of a reaction divided by time
85
Enzyme activity is:
The catalytic power of the enzyme
86
The catalytic power of the enzyme is indicated by an:
Increase in V
87
What is ΔG++?
Free Energy of Activation
88
Free Energy of Activation is always:
Positive, and lower with an enzyme
89
What is the Free Energy of Activation?
The energy required to reach the transition state of a chemical reaction
90
Can enzymes catalyze both directions of a reaction?
Yes
91
Enzymes ___ catalyze both directions of a reaction.
Can
92
What are the five factors that affect the rate of enzyme reactions?
Substrate concentration Enzyme concentration Temp pH Ionic strength
93
Substrate concentration Enzyme concentration Temp pH Ionic strength These five factors:
Affect the rate of enzyme reactions

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