proteins and enzymes Flashcards

1
Q

function of haemoglobin

A

allows oxygen to bind and be transported around the organism

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2
Q

function of antibody

A

binds to specific antigens
used in an organisms immume system response to a pathogen

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3
Q

function of enzymes

A

lowers Ea within a metabolic reaction

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4
Q

function of actin and myosin

A

involved in muscle contraction

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5
Q

function of keratin

A

found in nails for strength

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6
Q

how many types of amino acids

A

20

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7
Q

strcutre of an amino acid

A
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8
Q

bond between amino acids

A

peptide

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9
Q

primary structre

A

order and sequence of amino acids in a polypeptide chains

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10
Q

secondary structure

A

the way the polypeptide chain chain folds into
alpha helixes or beta pleated sheets
held together by weak H bonds

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11
Q

tertiary structure

A

further folding into specific 3D complex shape
r groups determine how it folds - ionic/weak H/disulphide bonds

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12
Q

what does the tertiary stucture determine

A

the shape of the protein is specific to its function and it determines how it interacts with other molecules

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13
Q

quaternary strcuture

A

consists of 2 or more polypeptide chains
globular or structural protein

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14
Q

denaturation of proteins

A

increasing temp increases kinetic energy of molecules, making them vibrate more
this can break weak H bonds in 2/3 strcuture
changing the pH breaks ionic bonds
this changes 3 strucutre

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15
Q

biuret test for proteins

A

2cm3 of biurets reagent with 2cm2 of sample
colour change is purple

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16
Q

what kind of protein is an enzyme

17
Q

how are products formed

A

when bonds are broken and reformed

18
Q

initial bond breaking requires

A

activation energy

19
Q

how do enzymes increase the rate of reaction

A

lower Ea for a chemical reaction

20
Q

how do enzymes lower the Ea

A

stressing bonds in the substrate during the formation of an enzyme substrate complex which allows reactions to occur at lower temps

21
Q

enzyme structure

A

active site
specific tertiary structure
specific complimentary shape to substrate

22
Q

lock and key model

A

active site is rigid and doesnt change
the substrate binds to the enzymes active site
substrate fits exactly to the active site (complimentary)
enzyme substrate complex reached, product formed and no longer fit into the active site so it released
enzyme is free to partake in another reaction

23
Q

induced fit model

A

substrate enters the enzymes active site and binds to it formin ESC
the binding of the subrate induces the change in the shape of the active site
the slight change in shape of the specific 3d tertiary stucture of the active site distorts the bonds within the substrate to lowers Ea of reaction
when substrate leaves, the active site returns to the original shape

24
Q

difference in induced fit model

A

active site isnt rigid
when substrate binds, the active site becomes more complimentary

25
enzyme conc as a factor affecting enzyme action
inititially ROR increases because the ESC being formed per sec increases eventually the graph plateus as the substrate becomes the limiting factor
26
substrate conc as a factor affecting enzyme action
inititially ROR increases because the ESC being formed per sec increases eventually the graph plateus as the enzyme becomes the limiting factor all the enzyme active sites fully occupied maximum number of ESC formed per sec
27
pH as a factor affecting enzyme action
as pH moves away from the optimum the ionic bonds in the tertiary structure are altered altering the shape of the active site active site is no longer complimentary to the substrate less/no ESC can form
28
temperature as a factor affecting enzyme action
as temp increases the kinetic energy increases more successful collisions, more ESC form increases the ROR at optimum temp the maximum number of ESC are formed per sec past the optimum the weak H bonds break changing the tertiary structure of the enzyme making the active site no longer complimentary to the substrate less/no ESC can form
29
conc of competitive inhibitor as a factor affecting enzyme action
at both high and low concentrations, the rate will eventually reach the same as without an inhibitor as enough substrate is added low conc will require less substrate added to overcome the inhibition and reach the maximum rate of reaction high conc will require more substrate added to overcome the inhibition and reach the maximum rate of reaction
30
conc of non competitive inhibitoras a factor affecting enzyme action
the maximum rate of reaction will never reach the same maximum rate of reaction as it would with no inhibitor present the maximum rate will be lower at a higher concentration of non competitive inhibitor
31
what are inhibitors
substances which decrease the ROR
32
competitive inhibitors
have a similar structure to substrates they bind to the active site temporarily prevent the substrate from bidning some product formed but takes longer than without the inhibitor can be overcome by increasing substrate concentration
33
non competitive inhibitors
binds to allosteric site causes a change to the shape of enzyme so substrates cannot bind
34
Describe the induced fit model of enzymic action
1. (before reaction) active site not complementary to substrate; 2. Shape of active site changes as substrate binds/as enzyme-substrate complex forms; 3. Stressing/distorting bonds (in substrate leading to reaction);