Polypeptides (proteins) Flashcards

1
Q

label an amino acid.

A

Carboxylic group (-COOH)

Amino group (-NH2)

One of 20 different ‘R groups’

Many amino acid (monomers) can be bonded together to form a polypeptide (polymer)

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2
Q

Explain the formation of a dipeptide.

A

2 amino acid molecules.

Condensation reaction.

Between the -COOH group of one amino acid and the -NH2 group of another.

A water molecule is released.

Forming PEPTIDE bond.

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3
Q

Name the four types of amino acid R-groups.

A

Ionic (+ or -)
Cysteine (-S)
Hydrogen bonding (-OH ….)
Hydrophobic (-CH3)

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4
Q

Primary structure

A

the sequence / order of amino acids in a polypeptide chain

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5
Q

Secondary structure

A

localised folding forming alpha helix / beta pleated sheet, stabilised be hydrogen bonding between the peptide bonds in the chain

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6
Q

Tertiary structure

A

precise 3D shape of a single polypeptide, stabilised by R-group interactions (i.e. hydrogen bonding, disulphide links, ionic interactions, hydrophobic interactions)

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7
Q

Quaternary structure

A

2 or more polypeptides bonded together (R - group interaction)

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8
Q

Explain the formation of a disulphide bond.

A

STRONG, COVALENT bond.

Between the R-groups…

… of 2 CYSTEINE amino acids

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9
Q

the food test for proteins.

A

Add Biuret reagent I (copper sulfate solution)

Add Biuret II (dilute sodium hydroxide solution)

Colour change from light blue to purple

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10
Q

What are the key features of globular proteins like haemoglobin

A
  • Polypeptide chains form a - spherical shape.
  • Often soluble
  • Hydrophilic R groups on the outside, hydrophobic on the inside
  • Sensitive to temperature and pH changes
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11
Q

What are the key features of fibrous proteins like collagen

A

Polypeptide chains are parallel
Tensile with a structural role

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