Protein and enzymes Flashcards

1
Q

draw the structure of an amino acid

A

-amine group
-r group
-carboxylic acid group
-hydrogen

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2
Q

dipeptide

A

-two amino acids joined
-via a condensation reaction
-joined by a peptide bond

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3
Q

primary structure

A

-the order/number/sequence of amino acids

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4
Q

secondary structure

A

-the way the chain is folded into
-beta pleated cheated
-alpha helical
-held together by hydrogen bonding

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5
Q

tertiary structure

A

-further folding into complex 3D specific structure held together by bonds between R-groups of different amino acids
-HYDROGEN between HO
-IONIC between +/- R groups
-DISULPHIDE bridges
-makes the protein specific to its structure

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6
Q

quaternary structure

A

-two or more polypeptide chains

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7
Q

test for proteins

A

-place sample in a test tube
-add equal volumes of Biuret solution
-colour change to purple shows protein is present

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8
Q

Enzyme action and definition

A

-enzymes are globular proteins which act as biological catalysts
-increase the rate of reaction
-lowering the activation energy
-done by stressing the bonds during the formation of the ESC

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9
Q

lock & key model

A

-active site is rigid and does not change shape
-substrate binds to enzymes active site
-substrate fits exactly to the complementary active site
-products are formed so are released as no longer fit the active site
-enzyme free to take part in another reaction

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10
Q

induced fit model

A

-active site not complementary
-active site changes shape as the substrate binds
-so stressed the substrate bonds to lower the Ea of the reaction
-active site returns to its original shape

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11
Q

effect of temperature on ROR

A

-increase in temp
-increase in kinetic energy
-more successful collisions
- more ESC form per second
-denaturation: past the optimum the hydrogen/ionic bonds will break causing a change in tertiary structure causing a change in the active site
-active site is no longer complementary so less ESC

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12
Q

effect of pH

A

-enzymes have an optimal pH
-if made more acidic or more basic
-charge on R groups are changed
-ionic bonds are broken
-tertiary structure is changed
-active site changes shape
-no longer complementary
-less ESC formed

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13
Q

effect of substrate conc. on graph

A

-increases
-plateaus
-as enzyme becomes the limiting factor

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14
Q

effect of enzyme conc. on graph

A

-increases
-plateaus
-as substrate becomes the limiting factor

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15
Q

competitive inhibitors

A

-similar shape to substrate
-binds to active site
-less ESC
-less product formed

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16
Q

non-competitive inhibitor

A

-not a similar shape to the substrate
-inhibitor binds to the allosteric site
-changes the shape of the active site
-less ESC
-less product formed

17
Q

activation energy

A

minimum energy required for a successful chemical reaction