3.1.4.1 proteins Flashcards

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1
Q

what is the monomer of a protein?

A

amino acid

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2
Q

what are the three groups that make up an amino acid?

A
  • amine group (NH₂).
  • r group.
  • carboxyl group (COOH).
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3
Q

how many different R groups/ amino acids are there?

A

20

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4
Q

what is a chain of amino acids called?

A

polypeptide chain.

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5
Q

how is a dipeptide formed?

A
  • the formation of two amino acids by a condensation reaction.
  • formed between a carboxyl and amine group.
  • releases water.
  • forms a peptide bond.
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6
Q

what kind of bond forms between two amino acids?

A

peptide bond.

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7
Q

how can a dipeptide be broken apart?

A

by a hydrolysis reaction which requires water.

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8
Q

what is the primary structure of a protein?

A

a long chain of amino acids held together by peptide bonds, in which the order and sequence of amino acids are key in determining the positions of the R groups and therefore the 2D and 3D shapes formed.

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9
Q

what is the secondary structure of a protein?

A
  • when the amino acid chain folds into either an alpha helix or beta-pleated sheet.
  • what causes the chain to fold up is the hydrogen bonds between the R groups.
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10
Q

what is the tertiary structure of a protein?

A
  • when the polypeptiode chain folds up into a complex, specific 3D shape.
  • this is due to various forces of attraction between the R groups.
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11
Q

what does the tertiary structure determine?

A

whether a protein is globular or fibrous.

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12
Q

what is the quaternary structure of a protein?

A
  • it is made up of two or more polypeptide chains.
  • the polypeptide chains are held together by the intermolecular forces between the R groups.
  • quaternary structures may involve prosthetic groups.
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13
Q

what type of forces are in the primary structure of proteins?

A

peptide bonds

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14
Q

what type of forces are in the secondary structure of proteins?

A

peptide and hydrogen

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15
Q

what type of forces are in the tertiary structure of proteins?

A

peptide, hydrogen, ionic, disulphide, london.

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16
Q

what type of forces are in the quaternary structure of proteins?

A

peptide, hydrogen, ionic, disulphide, london.

17
Q

what are hydrogen bonds?

A

the weak attraction between slightly positive H+ ions and the slightly negative O/N/F ions.

18
Q

what can break hydrogen bonds?

A

high temperatures or altered pHs.

19
Q

what are ionic bonds?

A

the electrostatic attraction between negative and positive ions.

20
Q

what can break ionic bonds?

A

changing pH.

21
Q

what are disulphide bridges?

A

STRONGEST BOND
covalent bonds between sulfur molecules and cystine R group.

22
Q

how can disulphide bridges be broken?

A

by reducing agents.

23
Q

what are london forces?

A

the weak forces of attraction between non-polar R groups.

24
Q

what can break london forces?

A

an increase in temperature.

25
Q

what are some examples of globular proteins?

A

enzymes and haemoglobin.

26
Q

what are some examples of fibrous proteins?

A

collagen and keratin.

27
Q

how many chains is haemoglobin made up of?

A

4 polypeptide chains.
= 2 beta chains and 2 alpha chains.

28
Q

what are some characteristics of haemoglobin?

A
  • 4 prosthetic haem groups.
  • globular protein.
  • soluble.
  • has hydrophilic parts on the outside.
29
Q

what are some characteristics of fibrous proteins?

A

insoluble in water = good for structure and support

30
Q

what is the test for proteins?

A

biuret test:
positive colour from blue to purple.