Protein Bonds In Protein Structure Flashcards

1
Q

Which bonds maintain protein primary structure?

A

Covalent peptide bonds

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2
Q

Which bonds maintain protein secondary structure?

A

Hydrogen bonds

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3
Q

Which bonds maintain protein tertiary and quaternary structure?

A
  1. Covalent disulphide
  2. Ionic
  3. H bonds
  4. Van der Walls
  5. Hydrophobic
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4
Q

What are disulphide bonds and in which proteins are they commonly found?

A
  • Strongest (214 kJ/mol)
  • Formed between Cys residues: lose 2H+ and 2e- (from -SH -SH to -S -S).
  • Limits protein folding but helps maintain structure.
  • Present mainly in proteins that are secreted or in hostile environment (e.g. Ribonuclease in the gut)
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5
Q

What can disulphide bonds be broken by?

A

Reducing agents, e.g. Beta-mercaptoethanol.

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6
Q

What are electrostatic interactions?

A
  • Relatively weak, 10-30 kJ/mol

- Formed between charged groups (salt bridges), e.g. Glu-, Asp- and Arg+, Lys+

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7
Q

What are hydrogen bonds?

A
  • Polarised, 10-30 kJ/mol

- Formed between an electronegative atom and a hydrogen bound to another electronegative atom.

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8
Q

What is the hydrophobic effect?

A
  • ~10kJ/mol

- Interaction between hydrophobic side chains due to displacement of water.

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9
Q

What are van dear Wales forces?

A
  • 4 kJ/mol
  • dipole-dipole interactions
  • Important when surfaces of 2 large molecules come together.
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10
Q

What is protein denaturation?

A
  • Disruption of protein structure due to breaking of forces holding proteins.
  • E.g. Heat increases vibrational energy
    pH alters ionisation state of aa and changes ionic/H bonds
    Organic solvents disrupt hydrophobic interactions
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11
Q

Describe the process of protein folding.

A
  • Ordered process (or would take too long)
  • Each step involves localised folding with stable conformations maintained
  • Driven by need to find most stable conformation.
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12
Q

Name diseases caused by protein misfolding.

A
  • AMYLOIDOSES involve amyloid fibres
    • misfolded, insoluble form of normally soluble protein
    • highly ordered with a high degree of beta-sheet

E.g. Alzheimer’s, T2 diabetes, Parkinson’s, Spongiform encephalopathies

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