MODULE 2 - PROTEINS Flashcards

(31 cards)

1
Q

How are peptide bonds formed?

A

through a condensation reaction

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2
Q

where does a peptide bond form between two amino acids?

A

between the N and C of the two aminos

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3
Q

what is a polypeptide?

A

when many amino acids are joined together by peptide bonds

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4
Q

which enzyme catalyses the formation of polypeptides?

A

peptidyl transferase

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5
Q

what is the primary structure of a protein?

A

the sequence of amino acids in a polypeptide chain

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6
Q

what bonds are involved in the primary structure of a protein?

A

peptide bonds

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7
Q

what are the secondary structures of a protein?

A

a-helices and b-pleated sheets

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8
Q

what bonds are involved in the secondary structures of a protein?

A

peptide and hydrogen bonds

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9
Q

what happens to the peptide chain to form a a-helix?

A

it twists/coils

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10
Q

what happens to the peptide chain to form a b-pleated sheet?

A

it folds

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11
Q

how is the tertiary structure of a protein achieved?

A

through the interaction of r groups on different amino acids. the folding and coiling of secondary structure formations brings the r groups close enough to interact and fold further

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12
Q

what 4 interactions can happen between r groups in tertiary protein structures?

A
  • hydrogen bonding
  • van Der walls forces
  • ionic bonds
  • covalent disulphide bonds
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13
Q

what are van Der walls forces?

A

weak interactions between polar and non-polar r groups

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14
Q

where do disulphide bonds form?

A

between r groups containing sulphur atoms, between the sulphur atoms

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15
Q

when can a protein from a quaternary structure?

A

when it has more than one polypeptide chain

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16
Q

what interactions occur in quaternary protein structures?

A
  • hydrogen bonding
  • van Der walls forces
  • ionic bonds
  • covalent disulphide bonds
17
Q

where do the interactions in quaternary protein structures take place?

A

between different protein molecules

18
Q

what is a prosthetic group?

A

a non-protein molecule (organic or inorganic) that binds tightly, often covalently, to a protein or enzyme

19
Q

what is a globular protein?

A

a compact, roughly spherical protein that’s generally water-soluble, folding into a specific 3D shape where hydrophobic (water-fearing) parts tuck inside and hydrophilic (water-loving) parts face outwards

20
Q

what is a conjugated protein?

A

a globular protein with a prosthetic group

21
Q

what is an example of a globular and conjugated protein?

22
Q

what is the structure of haemoglobin

A
  • 4 haem prosthetic groups each containing iron
  • has 4 polypeptide chains
23
Q

what is insulin an example of?

A

a globular protein (a hormone)

24
Q

give an example a conjugated protein which is an enzyme

25
what is the role of catalase?
to break down hydrogen peroxide which is a damaging byproduct of metabolism
26
list the properties of fibrous proteins
- insoluble due to their hydrophobic r groups - little/no tertiary structure - highly repetitive sequence very organised structures makes them strong
27
what is the function of keratin?
providing structural integrity, protection, and toughness to the outer layer of skin, hair, nails, feathers, and horns
28
what is the function of collagen?
to provide structure, strength, elasticity, and support to the body's connective tissues
29
what is the function of elastin?
to provide elasticity and recoil to tissues, allowing them to stretch and snap back to their original shape
30
what are the positive inorganic ions involved in biological processes?
Na+, Ca2+, K+, H+, NH4+
31
what are the negative inorganic ions involved in biological processes?
OH-, Cl-, HCO3-, PO43-, NO3-