eww look you're all zyme Flashcards

1
Q

what type of proteins are enzymes

A

globular

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2
Q

what are catalysts

A

alter the rate of chemical reactions without undergoing permanent change themselves

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3
Q

do the free energies of the products or reactants in a catalytic reaction have to be lower

A

products must be lowerrrrrr

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4
Q

what does evry chem reaction require

A

AE

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5
Q

do enzymes lower AE, what does this mean

A

yes, work at lower temps, metabolic processes work faster

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6
Q

what is the active site of an enzyme made of?

A

relatively small number of AAs - it is a small depression within the much larger enzyme molecule

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7
Q

where does a substrate fit into

A

enzyme-substrate complex

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8
Q
A
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9
Q

how is the substrate and enzyme bonded together

A

temporarily between the AAs in the enzyme active site and the groups in the substrate molecule

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10
Q

what does induced fit model suggest

A

that the active site of an enzyme forms as the substrate interacts and moulds around the substrate molecule

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11
Q

how does the induced fit actually affect the enzyme

A

like a glove there is a general shape but it is able to put strain on substrate molecule to induce a catalytic reaction and change shape

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12
Q

what is the general affect of temp on enzymes

A

temp increase KE of molecules and they will collide more frequently with enzymes’ active sites = more collisions = more enzyme-substrate complexes being formed and so the rate of reaction will increase but with a perpetual increase in temp the hydrogen bonds will begin to break and this will alter the shape of the active - at about 60 degrees it is so disrupted that is has denatured

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13
Q

how does pH affect the active site

A

a change in pH alter the charge of the amino acids in the active site - as a result the substrate can no longer be attached to the active site and the so the enzyme substrate complex can no longer be formed

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14
Q

what about a significant change in pH what would that do to an enzyme

A

it could cause the tertiary structures bonding to break - the active site would therefore be change and the es complex cannot be formed

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15
Q

will a change in pH denature an enzyme

A

no probs only will reduce activity

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16
Q

Define competitive inhibition

A

They have a similar shape to that of a substrate molecule

17
Q

Non competitive inhibitors, what are they

A

Do not bond to the active site as they have a different shape to the substrate so do not compete - bind to a site away from the active site known as the allosteric site - this causes the active the active site of the enzyme to change shape so it is no longer complimentary to the to the substrate - the es complex can no longer be formed.

18
Q

How will enzyme conc affect the rate of a catalytic reaction

A

Increasing enzyme conc increases the number of active sites available and for the substrate to collide with.
More ES complexes can form as enzyme conc increases

19
Q

what is a fibrous protein

A

they form long chains which run parallel to one another. these chains are linked by cross bridges and so form very stable molecules - one example is collagen

20
Q

what is the structure of collagen

A

its primary structure is an unbranched polypeptide chain
- the secondary structure is a polypeptide that is very tightly wound
- lots of amino acid and glycine helps with close packing
- in the tertiary the chain is twisted into a second helix.

  • quaternary is made up of three such polypeptides chains wound together like a rope
21
Q
A