PROTEINS Flashcards

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1
Q

what is proteins made up of

A

amino acids

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2
Q

what does the NH2 represent in an amino acid

A

amine group

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3
Q

what does the COOH represent in an amino acid

A

carboxylic group

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4
Q

what bond is formed in a condensation reaction between amino acids

A

peptide bonds

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5
Q

what are dipeptides

A

two amino acids joined together

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6
Q

what are polypeptides

A

multiple amino acids joined together

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7
Q

what is the structure of a primary protein

A

it is a straight chain of amino acids

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8
Q

structure of secondary protein

A

its is joined by hydrogen bonds when straight chain of amino acids have folded

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9
Q

structure of tertiary protein

A

3d structure when the the secondary protein has folded again causing ionic bonds disulphide bridges and more hydrogen bonds.

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10
Q

structure of quaternary protein

A

when two or more polypeptide chains have joined together held together by more ionic bonds , disulphide bridges,

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11
Q

how do you test for proteins

A

biuret test

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12
Q

explain the test for protein method

A

place biuret solution into a test tube with substance

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13
Q

what result do you expect to see if a protein is present

A

it will turn purple

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14
Q

what is the function of protein in relation to its structure.

A

it is involved in metabolic reactions. eg an enzyme has a tertiary structure which has a specific shape

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15
Q

what do enzymes do

A

they are biological catalysts which lower the activation energy.
- increase rate of reaction

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16
Q

list the properties of an enzyme

A

it has a tertiary structure so it is able to change shape

17
Q

what affect does the – enzyme concentration have on the rate of reaction `
what happens after a few minutes to the ror

A

enzyme concentration increases the rate of reaction

  • this is because there is more active sites to fit with the substrate
  • over time is decreases as the substrates have all been used up and is in excess
18
Q

what affect does the substrate concentration have on the rate of reaction

A

increases rate of reaction

  • as there are more substrates to fit into the active sites.
  • enzyme limiting factor- as there might not be enough active sites to fit into substrates so rate of reaction decreases.
19
Q

what affect does the concentration of competitive inhibitors on the rate of reaction

A

it decreases rate of reaction as competitive:
- bind to active site as it has a similar substrate shape so less enzyme substrate complexes are formed so less reactions

20
Q

what affect does the concentration of the non competitive inhibitors rate of reaction

A

non competitive:
changes the shape of active sites so less substrates can fit into it.
so less substrates will fit into the active site

21
Q

what affect does the PH have on the rate of reaction

A

the ph. increases the rate of reaction until it has reached its optimum level
- after optimum level the rate of reaction decrees as the enzymes denature

22
Q

what affect does the temperature have on the rate of reaction.

A

it increases as there are more kinetic energy causing more collisions
after optimum temp the rate of reaction decreases as the enzymes denature.

23
Q

what is competitive and non competitive inhibitors

A

competitive:

  • bind to active site as they have a similar substrate shape
  • this causes less substrates to bind to the active site of enzymes.

non competitive:

  • bind to other site of enzyme
  • causes active site to change shape
  • less substrates can fit into active site as there are different shapes.