Proteins, Enzymes And Digestion. Flashcards

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1
Q

What is a micelle?

A

And emulsified lipid droplet, coated with bile salts to prevent reformation.

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2
Q

Proteins are large molecules. True/false?

A

True

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3
Q

How are polypeptides formed?

A

Joining amino acid monomer units.

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4
Q

What 4 groups is the central carbon in an amino acid attached to?

A
  • amino group
  • carboxyl group
  • hydrogen
  • R ( side group, variety of chemical groups )
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5
Q

How are dipeptides formed?

A

In a condensation reaction with amino acid monomers.

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6
Q

What happens during a condensation reaction between two monomers in reference to the 4 chemical groups attached to the central carbon?

A
  • OH is removed from the carboxyl group of one amino acid.

- H removed from other amino acid

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7
Q

How can polypeptides be broken down?

A

Hydrolysis reaction

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8
Q

What is the primary structure of a protein?

A

A polypeptide

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9
Q

What does the primary structure of a protein do?

A

Determines the shape of the protein and its function

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10
Q

What bond joins monomers?

A

Peptide bond

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11
Q

Why are polypeptides able to form hydrogen bonds in the secondary structure of a protein?

A

There is an -NH and a -C=O group on either side of the peptide bond, the H is slightly electropositive, the O is slightly electronegative.

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12
Q

What shape is caused in the secondary structure of a protein as a result of the hydrogen bonds formed?

A

It becomes twisted into a 3D shape, e.g. A coil (alpha helix)

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13
Q

What re the two variations of proteins?

A

Fibrous and globular.

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14
Q

What is the tertiary structure of a fibrous protein?

A

Unbranched polypeptide chain that has been tightly wound and packed together closely by glycine, and then twisted into a second helix.

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15
Q

Name a fibrous protein.

A

Collagen

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16
Q

What us the quartenary structure of a fibrous protein?

A

3 polypeptide chains wound together similarly to fibres in a rope.

17
Q

What does collagen do?

A

Joins muscles and bones.

18
Q

Name examples of globular proteins and what they do.

A

Enzymes and haemoglobin

Carry out metabolic functions

19
Q

What type of protein are enzymes?

A

Globular

20
Q

What conditions must be present for a biochemical reaction to occur?

A
  • for substrates to collide in order to react they require sufficient energy
  • energy of products must be less than reactants
  • activation energy
21
Q

What does the protein biruet test detect?

A

Polypeptide bonds

22
Q

What are the steps to the protein biruet test?

A
  • place sample in test tube, add equal volume of sodium hydroxide at room temp.
  • add a few drops of dilute copper sulphate solution and mix
23
Q

What is the positive and negative result of a protein biuret test?

A

Positive - purple

Negative - blue

24
Q

Which part of the enzyme is functional?

A

The active site

25
Q

What is formed when the substate bonds with the enzyme’s active site?

A

Enzyme-substrate complex

26
Q

How does the induced fit model work?

A

The enzyme is flexible and changes shape in the presence of the substate.

27
Q

How does the induced fit model suggest the enzyme lowers the activation energy?

A

When altering in shape, it puts a strain on substate distorting a particular bond in the substrate, changing the activation energy.

28
Q

What is the secondary structure of a protein?

A

Alpha helix of beta pleated sheets held together by hydrogen bonds.

29
Q

What is the quaternary structure of a protein?

A

2 or more polypeptides held together.

30
Q

What is an example of a quaternary globular protein?

A

Haemoglobin, chlorophyll.

31
Q

What is the tertiary structure of a globular protein?

A

Secondary structure folded and held together by ionic, hydrogen and disulphide bonds?