Proteins Flashcards

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1
Q

What is the monomer of proteins?

A

Amino acids.

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2
Q

What polymer do amino acids form?

A

Polypeptides.

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3
Q

How many amino acids occur naturally in proteins?

A

20/ about 100 identified- this is indirect evidence for evolution.

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4
Q

What is the amino group?

A

(-NH2) - The basic group from which the ‘amino’ part of the name is derived.

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5
Q

What is the carboxyl group?

A

(-COOH) - An acidic group which gives the ‘acid’ part of the name.

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6
Q

What is the R group?

A

A variety of different chemical groups. Each amino acid has a different R group. This is where amino acids differ from each other.

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7
Q

How do amino acids form dipeptides?

A

Condensation reactions. - The water is made by combining the -OH from the carboxyl group and then -H from the amino group of another amino acid.

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8
Q

What bond holds two amino acids together?

A

Peptide bond. (Between the carbon atom of one amino acid and the nitrogen atom of the other.)

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9
Q

How can a peptide bond be broken?

A

Hydrolysis - this gives two constituent amino acids.

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10
Q

What does a sequence of amino acids in a polypeptide chain dictate?

A

The primary structure of a protein.

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11
Q

What is the sequence of amino acids in a polypeptide chain determined by?

A

DNA.

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12
Q

What does the primary structure determine?

A

Shape and hence function of protein.

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13
Q

What charge does the hydrogen of the -NH group have?

A

Overall positive.

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14
Q

What charge does the O of the -C=O group have?

A

Overall negative.

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15
Q

What are the bonds between the -NH and the -C=O called? Are they weak or strong?

A

Hydrogen bonds, weak.

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16
Q

What do hydrogen bonds cause?

A

The polypeptide chain to be twisted into a 3-D shape, such as the coil known as an α-helix.

17
Q

What is the tertiary structure maintained by?

A

A number of different bonds.

18
Q

Which bonds are formed in the tertiary structure?

A

disulfide bridges, ionic bonds, hydrogen bonds.

19
Q

How strong are disulfide bridges?

A

Fairly strong and not easily broken.

20
Q

Where are the ionic bonds formed in a protein?

A

Between any carboxyl and amino groups that are not involved in forming peptide bonds. These are weaker than disulphide bonds and are easily broken by changes in pH.

21
Q

What is important when it comes to the function of a protein?

A

The 3-D structure as it makes each protein distinctive and allows them to recognise, and be recognised, by other molecules. It can then interact with them in a specific way.

22
Q

Describe the primary structure of a protein. What does it do?

A

Primary structure is a sequence of amino acids found in its polypeptide chains. This sequence determines properties and shape.

23
Q

Describe the secondary structure of a protein. What does it do?

A

The secondary structure is the shape which the polypeptide chain forms as a result of hydrogen bonding. This is most often a spiral known as the α-helix, although other configurations occur.

24
Q

Describe the tertiary structure of a protein. What does it do?

A

The tertiary structure is due to the bending and twisting of the polypeptide helix into a compact structure. All three types of bond contribute to the maintenance of the tertiary structure.

25
Q

Describe the quaternary structure of a protein. What does it do?

A

The quaternary structure arises from the combination of a number of different polypeptide chains and associated nonprotein (prosthetic) groups into large, complex protein molecule, e.g., haemoglobin.

26
Q

Which protein test is used?

A

The Biuret test.

27
Q

Explain how to carry out the biuret test.

A

1) sample + hydroxide solution at room temp in test tube
2) Add a few drops of copper (II) sulfate solution
3) A purple colour indicates the presence of protein. Otherwise remains blue.

28
Q

What determines the 3-D shape of a protein?

A

The primary structure.