Honor Bio 7.1 Flashcards

1
Q

What are the similarities in the structure of all amino acids?

A

All amino acids have a central carbon atom (alpha carbon), an amino group (-NH₂), a carboxyl group (-COOH), a hydrogen atom, and a unique R group (side chain).

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2
Q

What are the differences in the structure of amino acids?

A

Different R groups.

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3
Q

What defines the primary structure of a protein?

A

The sequence of amino acids in a polypeptide chain.

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4
Q

What is the secondary structure of a protein?

A

Folding into alpha-helices and beta-sheets stabilized by hydrogen bonds.

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5
Q

What characterizes the tertiary structure of a protein?

A

The 3D shape of a single polypeptide chain formed by interactions between side chains (R groups).

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6
Q

What is quaternary structure?

A

The arrangement of multiple polypeptide chains into a functional protein complex.

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7
Q

What happens during protein denaturation?

A

A protein loses its secondary, tertiary, and quaternary structure due to external stress (e.g., heat, pH changes), causing it to lose its function.

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8
Q

How do hydrophobic interactions contribute to tertiary structure?

A

Hydrophobic side chains cluster together in the interior of the protein, avoiding water.

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9
Q

How do hydrophilic interactions contribute to tertiary structure?

A

Hydrophilic side chains are exposed on the protein surface, interacting with water.

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10
Q

How do acidic and basic side chains interact in tertiary structure?

A

Acidic (-COO⁻) and basic (-NH₃⁺) side chains form ionic bonds, stabilizing the structure.

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11
Q

How do cysteine side chains contribute to tertiary structure?

A

Cysteine side chains form disulfide bonds (S-S), providing strong covalent links.

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12
Q

What is the role of enzymes in proteins?

A

Enzymes catalyze chemical reactions by lowering activation energy.

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13
Q

What is the function of structural proteins like collagen?

A

Provide support and shape to cells and tissues.

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14
Q

How do transport proteins like hemoglobin function?

A

Carry substances (e.g., oxygen) through the body.

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15
Q

What role do antibodies play as proteins?

A

They are involved in immune defense, recognizing and neutralizing pathogens.

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16
Q

Why and how would the structure and function of a protein change if a hydrophobic amino acid was substituted for a hydrophilic one?

A

Substituting a hydrophobic amino acid with a hydrophilic one can disrupt the protein’s tertiary structure by altering hydrophobic interactions, potentially causing misfolding and loss of function.

17
Q

How are the effects of protein denaturation different from the effects of a mutation?

A

Denaturation: Temporary loss of function due to structural changes; the primary structure remains intact.
Mutation: Permanent change in the amino acid sequence, potentially altering protein folding, structure, and function.