Proteins Flashcards

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1
Q

monomer of a protein

A

amino acid

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2
Q

roles of proteins

A
  • structural
  • catalytic
  • signalling
  • immunoogical
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3
Q

what do amino acids consist of

A
  • carbolxyic group
  • amine group
  • R group
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4
Q

how are dipeptides formed

A
  • thorough a condensation reaction that results in a peptide bond
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5
Q

how many amino acids are there

A

20

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6
Q

what is a polypeptide chain

A

a chain of amino acids joined by a peptide bond

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7
Q

what four levels of protein structure exist

A

primary
secondary
tertiarty
quaternary

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8
Q

Primary structre

A
  • a specific sequence of amino acids forming a polypeptide chain
  • is linear
  • peptide bonding
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9
Q

Secondary structure

A
  • polypeptide chains folds to form ALPHA HELIX and BETA BLEATED SHEET
  • hydrogen bonding
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10
Q

Tertiary structure

A

Qu- alpha helix or beta pleated sheet fold to form compact globule’s (3D form)

  • enzymes
  • hydrogen, ionic, disulphid bonding between the sulphur and the R group
  • hydrophobic and hydrophillic interations
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11
Q

Quarternary structure

A
  • 2 or more proteins in tertiary structure bonded together
  • e.g. hemoglobin, insulin, collagen, DNA polymerase
  • hydrogen bonds
  • ionic bonds
  • disulphide bonds
  • hydrophobic and hydrophyillic interactions
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12
Q

what is the amino acid sequence coded by

A

gene sequence

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13
Q

fibrous proteins

A
  • protein in an elgonated shape
  • secondary structure
  • structural function
  • insoluble in water
  • less sensitive to changes
  • example: collagen, actin, silk, keratin, etc.
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14
Q

globular protein

A
  • tertaiaty structure
  • enzymatic function
  • rounded/spherical
  • soluble in water
  • senstive to change
    e. g. catalase, haemoglobin, insulin, DNA polymerase
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15
Q

what is the proteome

A
  • each individual has a unique proteome
    all of the proteins produced by a cell, tissue or organ
  • are not fixed as different cells make different proteins
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16
Q

what is denaturation

A

breaking down of the protein structure due to extreme conditions

17
Q

causes for denaturation

A
  • temperature ( increases kinetic energy and motion)
  • pH (also causes damage, each protein has an optimal pH)
  • physica interference
  • salt concentraitons
18
Q

2 main types of proteins

A
  • fibrous

- globulr