L2- Protein summary Flashcards

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1
Q

how many different levels of protien strucutre

A
4
primary
secondary
tertiary 
quarternary
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2
Q

Primary

A

Structure and function

- peptide bonds

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3
Q

Secondary

A

Localised folding

- hydrogen bonds

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4
Q

Tertiary

A

ultimate folding of the protein

- disulphide, ionic, H bonds, Van Der Waals, hydrophobic

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5
Q

quartenrayr

A

multiple subunit

-disulphide, ionic, H bonds, Van Der Waals, hydrophobic

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6
Q

protein dentauration

A

losing confirmation of native state caused by breaking forces holding proteins together

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7
Q

what can denature proteins

A
  • heat (vibration)
  • pH (alters ionisation state of amino acids)
  • detergents/organic solvents (disrupts hydrophobic interaction
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8
Q

example of protein misfolding which ca. cause disease

A

Transmissible spongiform encephalopathy e.g. BSE, Kuru, CJD

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9
Q

protein folding is not

A

random- driven by the need to find the most stable conformation

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10
Q

forces involved in maintaining proteins structure

A
  • covalent
  • electrostatic
  • hydrogen
  • hydrophobic
  • van der waals
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11
Q

covalent bond e.g. peptide bond

A

covalent bonds are strong

- broken by a reducing agent

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12
Q

example of a covalent bond

A

disulphide bond between two cysteine

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13
Q

most proteins with disulphide bonds re

A

secreted e.g. ribonuclease

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14
Q

electrostatic interactsions

A

formed between electronegative atoms and a hydrogen bound to another electronegative atom

  • salt bridges
  • relatively strong
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15
Q

hydrogen bonds

A

electrostatic interactions between water and nitrogen, oxygen or fluorine

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16
Q

hydrophobic effect

A

interactions between hydrophobic side chains due to displaced water
- hydrophobic part will group together away from water

17
Q

van der waals

A

very weak

  • due to dipole dipole interactions
  • transient location of electrons at any given moment

intrinsic to any bond