Protein structure Flashcards

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1
Q

What is a protein?

A

Polymers of amino acids, joined together by peptide bonds

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2
Q

Describe how amino acids bond to form the primary structure of a protein

A

Condensation reaction between H (from amine) and OH (from carboxyl). A covalent peptide bond is formed between the two amino acids.

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3
Q

Describe how R groups interact to determine the tertiary structure of the protein

A
  • Some R groups repel, some attract
  • Disulphide bridges form between specific atoms
  • Hydrogen bonds form
  • Ionic bonds form between oppositely charged atoms
  • Hydrophilic R groups move to the outside of the molecule, in contact with water molecules inside the aqueous cell
  • Hydrophobic R groups move to the inside of the molecule, shielded from other water molecules
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4
Q

State two properties of collagen that make it suitable for its purpose

A
  • Strong
  • Flexible
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5
Q

Describe how you would user a biochemical test to show if a solution contained protein

A
  • Add biuret reagent to solution
  • Blue to lilac/purple indicates protein is present
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6
Q

What is hydroxylating

A

Introduce a hydroxyl group (OH-) into a molecule or compound

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7
Q

Which two substances are formed when amino acid molecules join together?

A
  • Water
  • Peptide
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8
Q

Explain how a change in the primary structure of a globular protein may result in a different 3D structure

A
  • Different sequence of amino acids
  • Tertiary structure changes
  • Different bonds in different places
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9
Q

Describe how the secondary structure of a polypeptide is produced by bonds between amino acids.

A
  • Hydrogen bonds (between NH group of one amino acid and C=O group
  • Forming beta plated sheets or alpha helix’s
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10
Q

What is the primary structure of a protein

A

The specific sequence of amino acids in a polypeptide chain

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11
Q

What is the secondary structure of a protein (2 marks)

A

The sequence of amino acids causes parts of a protein molecule to twist and bend into alpha helix shapes or beta pleated sheets.
Hydrogen bnonds hold the secondary structure

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12
Q

What is the tertiary structure of a protein (3 marks)

A

The further folding of the secondary structure
To form a unique 3D shape
Held in place by ionic, hydrogen and disulphide bonds between R groups

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13
Q

What is the quaternary structure of a protein

A

A protein made up of more than one polypeptide chain

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14
Q

Give an example of a protein with a quaternary structure

A

Haemoglobin is made up of 4 polypeptide chains

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15
Q

What happens when a protein denatures

A

Ionic and hydrogen bonds that hold the tertiary structure together break down. Unique 3D structure collapses back into secondary structure.

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16
Q

How are proteins denatured

A

Too high a temperature (too much kinetic energy)
Too high/low a pH (too many H+ or OH-)

17
Q

Explain the importance of the primary structure

A

If even one amino acid in the sequence is different then it will cause the ionic/hydrogen/disulphide bonds to form in a different location.
This results in a different 3D shape

18
Q

What is a Globular protein

A
  • Protein that is spherical in shape
  • Soluble in water
19
Q

Why are globular proteins soluble in water

A

They have hydrophilic amino acids on their surface so hydrophilic R groups can react with water molecules in the aqueous cytoplasm of a cell.

20
Q

What is the function of haemoglobin

A

To bind reversibly to oxygen

21
Q

Give three examples of globular proteins

A

Enzymes, hormones, haemoglobin

22
Q

What are fibrous proteins

A

Proteins that play a structural role (they are also insoluble)

23
Q

Give three places where you are likely to find fibrous proteins

A

Bones, tendons, walls of arteries

24
Q

Why is keratin useful

A
  • Found in outer surface of skin, hair and fingernails
  • It is very strong because it contains large volumes of the amino acid cysteine
  • Cysteine forms disulphide bridges in the protein structure which are very strong covalent bonds
25
Q

Why are fibrous proteins insoluble in water

A

Contain high volumes of amino acids with hydrophobic R groups

26
Q

Where do we find collagen

A

In tendons, which connect muscles to bones. And ligaments, which connect bones to each other

27
Q

What is the structure of collagen

A

Polypeptide chains in collagen wrap tightly together to form a triple helix

28
Q

Why can collagen polypeptides wrap very tightly around each other

A
  • Every third amino acid is glycine, which has a tiny R group of just a hydrogen atom, allowing for a large number of hydrogen bonds between the polypeptide chains. Which helps stabilise the quaternary structure of the protein
29
Q

What are collagen polypeptides chains joined together by

A
  • Many hydrogen bonds
  • Strong crosslinks
30
Q

What are the larger structures of collagen called

A

Microfibrils and fibrils

31
Q

How do microfibrils and fibrils avoid weak spots

A

The molecules are staggered so there aren’t gaps running along the structure (weak spots)