3.1.4.1 Proteins Flashcards

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1
Q

What is the monomer of proteins

A
  • amino acid
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2
Q

What chemical properties in proteins change

A
  • non-polar (hydrophobic)
  • polar (hydrophilic)
  • positive charge (hydrophilic)
  • negative charge (hydrophilic)
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3
Q

What is the polymer of proteins

A
  • polypeptide
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4
Q

How is a polypeptide formed

A
  • condensation reaction
  • between amine & carboxyl groups
  • forms peptide bond
  • water released
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5
Q

How do you break a polypeptide

A
  • hydrolysis
  • requires water
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6
Q

Describe the primary structure of proteins

A
  • sequence of a.a joined by peptide bond
  • controls the protein shape
  • varied:
    . Different length chains
    . Different a.a in chain
    . Amino aids in different sequences
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7
Q

Describe the secondary structure of proteins

A
  • folding of parts of chain - alpha helices or beta-pleated sheets
  • due to H2 bonding
  • between carboxyl & amino residues
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8
Q

Describe the tertiary structure of proteins

A
  • folding into complex, specific, shape
  • due to IMF between R groups
  • H2 bonds - between polar R groups
  • ionic forces - between + and - R groups
  • disulphide bridges - covalent bond between cysteine R groups
  • London forces - between non-polar R groups
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9
Q

describe the quaternary structure of proteins

A
  • holds the polypeptide chains together
  • due to IMF between R groups
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10
Q

What are the 2 groups of structures in proteins

A

Globular:
- enzymes, signalling molecules, transport molecules. Have a specific shape for binding

Fibrous:
- structural. Strong & flexible

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11
Q

What is the test for proteins

A
  • buret test
  • positive result: colour change from blue to purple
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