Proteins Flashcards

1
Q

how is a peptide bond formed

A

condensation between two amino acids

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2
Q

what are the monomers proteins are made from

A

amino acids

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3
Q

draw an amino acid

A
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4
Q

draw a dipeptide

A
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5
Q

how are dipeptides formed

A

condensation of two amino acids

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6
Q

how are polypeptides formed

A

condensation reaction between many amino acids

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7
Q

primary structure of proteins

A

sequence of amino acid chain

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8
Q

secondary structure of proteins

A

involves alpha helix and beta pleated sheets
- chains fold over
- hydrogen bonds

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9
Q

tertiary structure of proteins

A

folding into a 3D shape
- ionic bonds, disulphide bridges, hydrogen bonds

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10
Q

quaternary structure of proteins

A

more than one polypeptide chain binder together

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11
Q

what is the biuret test for proteins

A

add biuret solution
will turn purple if postive

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12
Q

what is the induced fit model of enzymes

A

when an enzyme substrate complex is formed, the structure of the enzyme is altered so the active site fits around the substrate

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13
Q

how does temperate affect enzyme action

A
  • increases temperature as kinetic energy of enzyme increases so particles move quicker and collide more > more ES complexes are formed
  • denatured after optimum
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14
Q

how does pH affect enzyme action

A
  • disrupts the bonds in the tertiary structure of the enzyme
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15
Q

how does enzyme concentration affect enzyme

A
  • more enzymes = more active sites for substrates to bind to
  • increases enzyme substrate complexes
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16
Q

how does substrate concentration affect enzymes

A
  • more substrates = more enzyme substrate complexes formed
17
Q

what is competitive inhibition

A
  • competitive inhibitors have a similar shape to substrate of enzyme
    > compete for active site so no ES complexes formed
18
Q

where does a non competitive inhibitor bind do

A

allosteric site

19
Q

what is formed when substrate and enzyme collide

A

enzyme substrate complex