Proteins Flashcards

(24 cards)

1
Q

How do monomers form the primary structure of a protein?

A

Condensation reaction between amino acids; forming peptide bonds; creating a specific sequence/order of amino acids.

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2
Q

What reaction joins amino acids to form a dipeptide?

A

Condensation (reaction) / loss of water.

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3
Q

What groups form the peptide bond in a dipeptide?

A

Between amine / NH₂ and carboxyl / COOH.

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4
Q

What determines the structure of a protein?

A

The (relative) position of amino acid/R group/interactions.

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5
Q

What interactions determine tertiary protein structure?

A

Hydrogen bonds / disulfide bridges / ionic bonds / hydrophobic-hydrophilic interactions.

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6
Q

What is the primary structure of a protein?

A

Sequence/order of amino acids.

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7
Q

What forms the secondary structure in a protein?

A

Hydrogen bonding between amino acids.

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8
Q

What shapes are part of the secondary protein structure?

A

Alpha helix / β-pleated sheet.

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9
Q

How is tertiary structure formed?

A

By interactions (between R groups): hydrogen bonds, disulfide bridges, ionic bonds, hydrophobic-hydrophilic interactions.

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10
Q

What does tertiary structure create in enzymes and other proteins?

A

Active site in enzymes OR complementary/specific shapes in antibodies/carrier proteins/receptors.

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11
Q

What is quaternary protein structure?

A

More than one polypeptide chain joined by interactions/bonds; may include a prosthetic group.

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12
Q

What are proteins made of?

A

Polymer of amino acids joined by peptide bonds, formed by condensation reactions.

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13
Q

What is the primary protein structure?

A

Number AND order of amino acids.

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14
Q

What is the secondary protein structure?

A

Folding of the polypeptide chain into Alpha-helix and Beta-pleated sheets due to hydrogen bonding.

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15
Q

What is the tertiary protein structure?

A

3-D folding due to hydrogen bonding, ionic bonding, and disulfide bridges.

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16
Q

What is the quaternary structure of proteins?

A

Two or more polypeptide chains joined together.

17
Q

How do you test for proteins in a solution?

A

Add Biuret solution; purple/lilac result indicates protein is present.

18
Q

What test confirms the presence of lipid?

A

Add ethanol/alcohol, then water and shake; white/milky emulsion confirms presence.

19
Q

How do you confirm a non-reducing sugar is present?

A

Do Benedict’s test and it stays blue; then boil with acid, neutralise with alkali; heat with Benedict’s → red/orange precipitate forms.

20
Q

How do you test for amylase in a sample?

A

Add Biuret reagent → purple/lilac; OR add starch, leave, and test for reducing sugar or starch absence.

21
Q

How do you distinguish lactase from lactose using the Biuret test?

A

Add Biuret reagent to both; lactase/enzyme = purple/lilac; lactose = stays blue.

Because: Lactase is a protein.

22
Q

Why doesn’t sucrase hydrolyse lactose?

A

Lactose has a different shape/structure; doesn’t fit/bind to sucrase’s active site; no enzyme-substrate complexes formed.

23
Q

Why doesn’t lactose bind to sucrase?

A

Active site of sucrase has a specific shape/structure; lactose doesn’t fit = no binding = no reaction.

24
Q

Draw the general structure of an amino acid