Topic 1---A: Biological molecules- 5. proteins Flashcards

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1
Q

What are the monomers of proteins?

A

Amino acids

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2
Q

How is a dipeptide formed?

A

When two amino acids join together

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3
Q

How is a polypeptide formed?

A

When more than 2 amino acids join together

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4
Q

What are proteins made up of?

A

1 or more polypeptides

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5
Q

Amino acid (structure)

A
  • Carboxl group (COOH)
  • Amine group (H2N)
  • R GROUP (1 of 20 varieties) attached to a carbon
  • R GROUP consists of 1 hydrogen atom
    H H O
    \ I //
    N -C-C
    / I \ OH
    H R
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6
Q

How are amino acids linked together to form dipeptides and polypeptides?

A

By condensation reaction between amine and carboxyl group so a molecule of water is released during the reaction.
- Peptide bond is formed between the amino acids

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7
Q

What are the bonds between amino acids called?

A

Peptide bonds

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8
Q

When does hydrolysis happen?

A

When dipeptides and polypeptides are broken down

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9
Q

How is there 20 different amino acids?

A

-Because there are 20 different R groups
- Each R group is slightly different so each amino acid has different properties so proteins have a wide range of properties.

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10
Q

What are the 4 levels of structure in a protein?

A
  • Primary
  • Secondary
  • Tertiary
  • Quaternary
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11
Q

Primary structure (proteins)

A

This is the sequence of amino acids in a polypeptide chain

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12
Q

Secondary structure (proteins)

A
  • Hydrogen bonds form between the amino acids in the chain between the amine and carboxyl groups
  • This makes it automatically coil into a alpha helix or fold into a beta pleated sheet
  • Hydrogen bonds hold the secondary structure in place
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13
Q

Tertiary structure (protein)

A
  • The coiled or folded chain of amino acids is often coiled and folded further.
  • More bonds form between different parts of the polypeptide chain including hydrogen and ionic bonds.
  • Disulphide bonds also form whenever 2 molecules of the same amino acid cysteine come together
  • For proteins made from a single polypeptide chain the tertiary structure forms their final 3D structure
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14
Q

Quaternary structure (protein)

A

-Protein made up of several different polypeptide chains held together by bonds
- It’s the way the polypeptide chains are assembled together

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15
Q

What is an example of a quaternary structure?

A

Haemoglobin (4 polypeptide chains associated together)

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16
Q

Why is the sequence of amino acids important?

A
  • They determine the tertiary structure so therefore the overall 3D shape of the molecule due to the bonds forming in different locations.
17
Q

What does a proteins shape determine?

A

Their function

18
Q

Enzymes (protein example)

A
  • Usually spherical in shape due to the tight-folding of the polypeptide chains.
  • Their soluble and have roles in metabolism like breaking down large food molecules.
19
Q

Transport proteins (protein example)

A
  • Channel proteins are present in cell membranes
  • They contain hydrophobic and hydrophilic amino acids
  • This causes the protein to fold up and form a channel so they can transport molecules and ions across cell membranes.
20
Q

Structural proteins (protein example)

A
  • Physically strong
  • Consist of long polypeptide chains lying parallel to each other with cross links between them.
  • E.g. keratin and collagen
21
Q

What happens when a protein denatures?

A
  • Hydrogen and ionic bonds in secondary and tertiary structure break
  • Lose the 3D shape
  • E.g. from changes in temperature/ PH
22
Q

Biuret test (proteins)

A
  1. Test solution needs to be alkaline so first you add a dew drops of sodium hydroxide solution
  2. Then add some copper (II) sulfate solution.
  3. If protein is present it will go from blue to purple
23
Q

Ionic bonds

A
  • Quite Strong
  • Form between R groups
24
Q

Hydrogen bonds

A
  • Weak
  • Easily broken by temperature or pH
25
Q

Disulphide bridges

A
  • Covalent (very strong)
  • Form between sulphur atoms in the R group of cysteine