Protein Note Flashcards

1
Q

What do proteins do in cells?

A

Do most of the work in cells

Proteins serve various functions including structural support, enzymatic activity, and transport.

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2
Q

How are proteins classified?

A

By function (ex: structure, enzyme, carrier)

Proteins can be classified based on their roles in biological processes.

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3
Q

What is the role of proteins as fuel?

A

Used as a fuel - excess may be burned as a last resort in crisis

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4
Q

What are proteins made of?

A

Chains of amino acids folded into specific 3D shapes

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5
Q

What determines a protein’s function?

A

A protein’s structural characteristics

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6
Q

How many different R groups are commonly found in living organisms?

A

20 different R groups

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7
Q

What term describes amino acids having both acidic and basic functional groups?

A

Amphiprotic

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8
Q

List the essential amino acids.

A
  • Histidine
  • Isoleucine
  • Leucine
  • Lysine
  • Methionine
  • Phenylalanine
  • Threonine
  • Tryptophan
  • Valine
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9
Q

What are essential amino acids?

A

Amino acids that cannot be synthesized by humans and must be consumed

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10
Q

What is a key deficiency in some plant proteins?

A

Some are lacking some amino acids in proper amounts for humans

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11
Q

What is a polypeptide?

A

A chain of amino acids (>10 aa)

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12
Q

What type of reaction connects amino acids?

A

Condensation reaction

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13
Q

Which end of the growing polypeptide chain do amino acids get added to?

A

Carboxyl end (C-terminus)

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14
Q

How are polypeptides broken down?

A

In a hydrolysis reaction

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15
Q

What is the primary structure of a protein?

A

Unique sequence of amino acids in a polypeptide chain

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16
Q

What determines the amino acid sequence?

A

DNA (the nucleotide sequence of a gene)

17
Q

What condition can result from changing one amino acid in a sequence?

A

Loss of function

18
Q

What is an example of a disease related to amino acid substitution?

A

Sickle Cell Anemia

19
Q

What characterizes secondary structure in proteins?

A

Immediate folding and formation of hydrogen bonds

20
Q

What are two types of secondary structures?

A
  • α-helix
  • β-pleated sheet
21
Q

What causes tertiary structure in proteins?

A

Forces of attraction and repulsion between the polypeptide and its environment

22
Q

What types of interactions contribute to tertiary structure?

A
  • Hydrogen bonds
  • Ionic bonds
  • Van der Waals forces
23
Q

What is the quaternary structure of a protein?

A

Two or more polypeptide chains come together to form a functional protein

24
Q

What is an example of a protein with quaternary structure?

A

Hemoglobin

25
What factors determine the final shape of a protein?
* Temperature * pH * Ionic concentration * Other factors
26
What is denaturation?
Change in protein shape due to environmental conditions
27
What is the role of enzymes?
Catalyze biological reactions
28
What is an example of a structural protein?
Actin
29
What do protein hormones do?
Regulate physiological processes
30
What is an example of a functional protein?
Hemoglobin
31
What do transport proteins do?
Move substances through membranes
32
Are the four levels of protein folding real stages?
No, they occur simultaneously while the protein is being synthesized
33
Name two functions of proteins.
* Catalyzing chemical reactions * Cell signaling
34
Which statement is accurate regarding protein structure?
D: Interactions between the R groups in amino acids form tertiary structure.
35
What happens to a protein during denaturation?
It loses its secondary structure and may revert to primary structure.