Proteins - structure Flashcards

(17 cards)

1
Q

What factors are proteins sensitive to that can affect their structure?

A

Temperature and pH changes

Proteins are sensitive to environmental changes, particularly temperature and pH, which can disrupt their structure.

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2
Q

What is the dependence of a protein’s precise structure?

A

Ionic interactions, hydrogen bonds, and other intermolecular forces between polypeptide chains

The precise structure of a protein is reliant on these interactions being intact.

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3
Q

What is denaturation in the context of proteins?

A

The irreversible change of protein conformation

Denaturation results in a permanent alteration in the protein’s structure.

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4
Q

How do temperature and pH extremes lead to denaturation?

A

They interfere with the bonds that maintain protein structure

Denaturation occurs when the bonds between R groups are disrupted.

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5
Q

What type of bonds are broken during denaturation?

A

Weak bonds between different R groups

These bonds are weaker compared to peptide bonds that hold amino acids together.

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6
Q

What can the altered shape of a protein affect?

A

Its function, physical state, and general usefulness

A protein’s altered shape due to denaturation can significantly impact its role.

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7
Q

What is considered an optimum pH for a protein?

A

A pH at which the protein’s 3D structure is not denatured

Proteins have specific pH levels where they maintain their structure.

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8
Q

Is denaturation reversible?

A

Almost always irreversible

Proteins cannot typically return to their original conformation after denaturation.

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9
Q

What small changes can some proteins undergo in response to pH fluctuations?

A

Small denaturations and renaturations

Some proteins can adapt to minor changes in pH.

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10
Q

What is an example of a protein that can undergo small denaturations?

A

Haemoglobin

Haemoglobin can respond to small fluctuations in pH.

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11
Q

How can denaturation be observed in cooking?

A

By changes in egg white when fried or poached

The protein albumin in egg whites undergoes denaturation with heat.

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12
Q

What happens to the hydrophobic amino acids in albumin during cooking?

A

They move to the edges, causing the protein to become insoluble

This leads to the formation of a solid layer in the cooked egg white.

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13
Q

What is the optimum pH of the enzyme pepsin?

A

pH 2

Pepsin functions optimally in the acidic environment of the stomach.

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14
Q

What type of organisms have evolved proteins that are stable at extreme conditions?

A

Extremophiles

These organisms can survive at extreme pH or temperature levels.

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15
Q

What is the significance of Thermus aquaticus?

A

It is a bacterium that lives in hot springs at 80°C

This temperature would denature most other proteins.

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16
Q

How can denaturation of enzymes be used in experiments?

A

To measure enzyme activity

Experiments can establish the optimum pH or temperature for enzymes.

17
Q

Why can’t many protein-based drugs be administered orally?

A

They will be denatured by stomach acid

These drugs require alternative delivery methods, such as injection.