3.6 Structure of proteins Flashcards

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1
Q

What are peptides?

A

Polymers made up of two or more amino acid molecules

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2
Q

What do proteins consist of?

A

One or more polypeptides arranged as complex macromolecules

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3
Q

*What elements do proteins contain

A

Carbon, hydrogen, oxygen, nitrogen

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4
Q

What are R-groups?

A

Variable groups on amino acids

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5
Q

How many amino acids are found in cells?

A

20

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6
Q

How many amino acids are non-essential? What does this mean?

A

5 - our body can make them from different amino acids

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7
Q

How many amino acids are essential? What does this mean?

A

9 - only obtainable from food

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8
Q

How many amino acids are conditionally essential? What does this mean?

A

6 - only needed by growing children

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9
Q

Describe what happens during synthesis of peptides

*(Refer to Figure 2 on p.g. 59)

A

-Amino acids join when amine and carboxylic acid groups react
-Hydroxyl in the carboxylic acid group of one amino acid reacts with a hydrogen in the amine group of another amino acid
-Peptide bond forms between amino acids and water is produced (this is an example of a condensation
reaction)
-The resulting compound is a dipeptide

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10
Q

What is a peptide bond?

A

The bond formed between 2 amino acids

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11
Q

What happens when many amino acids are joined by peptide bonds?

A

A polypeptide forms

Polypeptide - chains of 3 or more amino acids

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12
Q

What enzyme catalyses the reaction which forms peptide bonds?

A

Peptidyl transferase, found in ribosomes

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13
Q

Define R-group interaction. What does this result in?

A
  1. Different R-groups in the amino acids making up one protein can interact
  2. Forming different types of bonds
    -These bonds cause the long amino acid chains (polypeptides) to fold into complex structures
    (proteins)
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14
Q

What does the presence of different amino acid sequences lead to?

A

Different structures with different shapes being produced

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15
Q

Why does a protein’s shape have to be specific?

A

Vital for the protein to carry out its function

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16
Q

*What is thin layer chromatography (TLC) used for?

A

To separate individual components of a mixture

e.g. identify a mixture of amino acids in a solution

17
Q

*What are the 2 phases in TLC? What happens at each phase?

A
  1. Stationary phase
    - Thin layer of silica gel/any other adhesive substance is applied to a rigid surface e.g. sheet of glass
    - Amino acids are added to one end of the gel
    - This end is submerged in organic solvent
  2. Mobile phase
    - The organic solvent moves through the silica
18
Q

*What is the rate at which amino acids move dependent on?

A
  1. Interactions the amino acids have with the silica during the stationary phase
  2. Amino acid’s solubility during the mobile phase
    - Since these vary, the amino acids move different distances in the same period of time
19
Q

*How do you carry out the procedure to separate and identify a mixture of amino acids in solution?

A
  1. Whilst wearing gloves, draw a baseline 2cm from the bottom in pencil on the chromatography plate (handle the plate by its edges)
  2. Mark 4 equally spaced points along the baseline
    3.
20
Q

Explain what the primary structure of a protein is

A
  1. Sequence in which amino acids are joined
    - Directed by information carried within DNA
    - Amino acids in the sequence influence how the polypeptide folds to give the protein’s final shape - this determines its function
    - Only contains peptide bonds
21
Q

Explain what happens in the secondary structure of a protein

A
  • Oxygen, hydrogen and nitrogen atoms of the amino acid structure interact
  • Hydrogen bonds form within the amino acid chain, pulling it into a coil shape known as ‘alpha helix’
  • Result of hydrogen bonds
22
Q

What is the secondary structure a result of?

A

Hydrogen bonds

23
Q

Where does the secondary structure form?

A

At regions along long protein molecules, depending on the amino acid sequence

24
Q

What forms a beta pleated sheet?

A

Polypeptide chains parallel to each other joined by hydrogen bonds, forming sheet-like structures

25
Q

What happens in the tertiary structure?

A

The protein is folded into its final shape