Paper 1 - Proteins and Enzymes Flashcards

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1
Q

What are proteins?

A

Polymers made up of one or more chains of amino acid monomers

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2
Q

Amino acid structure

A

amino group - side chain - carboxyl group

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3
Q

What is a dipeptide ?

A

2 amino acids joined together with a peptide bond in a condensation reaction

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4
Q

Fibrous proteins

A
  • Long, thin molecules
  • insoluble in water
  • parallel chains + many cross linkages = long fibres
  • strong + stable
  • eg. Keratin in hair
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5
Q

Globular proteins

A
  • Compact
  • soluble in water
  • e.g. Enzymes, antibodies, haemoglobin etc
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6
Q

Test for proteins

A
  1. Add a few drops of biuret solution
    2.it present-colour change of pale blue to lilac
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7
Q

Primary structure of a protein

A

The sequence of amino acids in the polypeptide

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8
Q

Secondary structure of a protein

A
  1. Polypeptide chain coils into an alpha helix
  2. Polypeptide chain folds into a beta pleated sheet
  • hydrogen bonds
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9
Q

Tertiary structure of a protein

A

Folding of the secondary structure into a specific 3D shape = functional properties

  • disulphide, ionic, hydrogen bonds
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10
Q

Quaternary structure of a protein

A

More than one polypeptide chain eg. Hb

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11
Q

What are enzymes?

A

Globular proteins that act as biological catalysts

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12
Q

Lock and Key Model

A

Substrate (key) is complimentary to the active site (lock) so they bind perfectly

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13
Q

Induced fit model

A

The active site mould itself around the substrate and then becomes fully complementary = strain on the substrate and its bonds and lowers the energy needed to break the bonds

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14
Q

Immobilised enzymes

A

Enzymes that have been trapped into an inert matrix which prevents them from moving

  • Makes recovery and reuse of enzymes easier
  • Ensures that the enzymes doesn’t contaminate the final product
  • Allows for continuous processes
  • Offers enzyme stability in temp. and pH = greater efficiency
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15
Q

What are the factors affecting enzyme action?

A
  1. Temperature
  2. pH
  3. Substrate concentration
  4. Enzyme concentration
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16
Q

Temperature on Enzyme Action

A

Higher temperature:
- increase in kinetic energy of enzyme + substrate molecules
- collide with enough energy more frequently
- increases rate of reaction

17
Q

Explain denaturation

A

When optimum temperature is reached, hydrogen bonds break → changes tertiary structure of enzyme → alters shape of active site → substrate will no longer fit the active site ( no longer complimentary)

18
Q

pH on Enzyme Action

A
  • Increase / decrease = decrease in rate of enzyme activity
  • H+ ions affect the hydrogen + ionic bonds in enzymes which hold the tertiary structure
    → change in shape of active site
    → enzyme is no longer complimentary to the substrate
    → no ES complexes form
19
Q

Define pH

A

Concentration of hydrogen ions present in a solution

pH = -log10 H+

20
Q

Substrate concentration on Enzyme Action

A

As more substrate is added, all active sites become occupied - rate is at maximum = enzyme saturated → line plateaus

Substrate conc is no longer a limiting factor

21
Q

Enzyme concentration on Enzyme Action

A

As the conc increases, there are more active sites available to form ES complexes = rate of reaction increases

All substrates become occupied = enzymes in excess - free ones with no substrate to bind to

22
Q

Competitive inhibitors

A

Similar shape to substrate so can bind to the active site→ presents the substrate from entering it = no ES complexes formed

23
Q

Non-competitive inhibitors

A

Attach themselves to the allosteric site → altering the shape of the active site → substrate = no longer complimentary → no ES complexes formed