3.1.4.1 General properties of proteins Flashcards

(34 cards)

1
Q

what are the monomers from which proteins are made?

A

amino acids

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2
Q

what is the general structure of an amino acid (draw it out)?

A

NH2 represents an amine group, COOH represents a carboxyl group and R represents a side chain

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3
Q

what element does the R group in an amino acid generally contain?

A

carbon

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4
Q

which amino acid’s R group only contains hydrogen?

A

glycine

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5
Q

which amino acid’s R group contains sulfur?

A

cysteine

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6
Q

how many amino acids are common in all organisms?

A

20

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7
Q

what is the only way that the amino acids differ from each other?

A

the R (side) groups can differ

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8
Q

what reaction joins two amino acids?

A

a condensation reaction

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9
Q

what bond is formed when two amino acids combine?

A

a peptide bond

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10
Q

where is the peptide bond formed between two amino acids?

A

one amine group joins to a carboxyl group from another amino acid

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11
Q

how are dipeptides formed?

A

by the condensation reaction between the amine and carboxyl group of two amino acids

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12
Q

how are polypeptides formed?

A

by the condensation reaction between 2 or more amino acids

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13
Q

draw the formation of a dipeptide and circle the peptide bond?

A
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14
Q

what does a functional protein contain?

A

may contain one or more polypeptides

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15
Q

what is the structure of a protein determined by?

A

the position of amino acids / R groups / interactions

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16
Q

how many structural levels are there to proteins?

A

4 (primary, secondary, tertiary and quaternary)

17
Q

what is the primary structure of a protein?

A

the sequence and number of amino acids

18
Q

what is the secondary structure of a protein?

A
  • hydrogen bonds
  • forming an α-helix or a β-pleated sheet
19
Q

where do hydrogen bonds form in the secondary structure of a protein?

A

between NH group of one amino acid and C=O group

20
Q

what is the tertiary structure of a protein?

A
  • formed by interactions between R groups
  • the 3D shape of a polypeptide chain
  • this determines the function of the protein
21
Q

which bonds are involved in the tertiary structure of a protein?

A
  • hydrogen bonds
  • ionic bonds
  • disulfide bridges
  • covalent bonds
  • hydrophobic interactions
    –> these are all known as ‘interactions’
22
Q

which bonds maintain the tertiary structure of a protein?

A
  • hydrogen bonds
  • ionic bonds
  • disulfide bridges
23
Q

what is the property of hydrogen bonds in proteins?

A

they are numerous but easily broken

24
Q

what is the property of ionic bonds in proteins?

A

they are weaker than disulfide bonds and are easily broken by changes in pH

25
where do ionic bonds form?
between R groups of different amino acids
26
what is the property of disulfide bridges in proteins?
they are resistant to chemical and physical attack and therefore cannot be easily broken
27
where do disulfide bridges form?
between R groups of different amino acids
28
what is the quaternary structure of a protein?
- more than one polypeptide chain - other non-protein groups can also be associated - formed by interactions between polypeptides
29
what is the function of fibrous proteins?
structural (collagen)
30
what is the function of globular proteins?
metabolic (haemoglobin / enzymes)
31
what does it mean if a protein is denatured?
- bonds which hold the secondary and tertiary structure break - unique 3D shape is lost
32
what are the conditions that denature a protein?
- too high a temperature (too much kinetic energy can break intermolecular bonding) - too high / low a pH (too many H+ or OH- ions can disrupt ionic charges in R groups)
33
what happens if one amino acid changes in the primary structure of a protein?
- different sequence of amino acids - causes hydrogen / ionic / disulfide bonds to form in a different place - this results in a different 3D shape
34
what is the food test for proteins?
- add biuret's solution to sample - if protein is present, colour change from blue to purple