unit 3: enzymes and proteins Flashcards

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1
Q

what are proteins made from

A

C , H , O , N AND S

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2
Q

What are proteins

A

polymers of a long chain of monomers called amino acids

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3
Q

how many natural occurring proteins are there

A

20

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4
Q

what are properties of amino acids determined by

A

amino acid sequence of the protein and the way the protein is folded

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5
Q

give examples of proteins functions

A

haemoglobin , antibodies , enzymes

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6
Q

what is the amino acid sequence

A

R
H2N-C-COOH
H

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7
Q

how do amino acids differ

A

by their R groups

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8
Q

how are amino acids linked together

A

through a condensation reaction to form dipeptides and polypeptides

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9
Q

what do condensation reactions do with water

A

release water

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9
Q

when does hydrolysis occur

A

when dipeptides and polypeptides are broken down , use water

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10
Q

what happens during a condensation reaction of amino acids

A

-the amino acids line up
-amine group of one amino acid lines up with the carboxyl group of another
-amine group donates 1 H atom
-carboxyl group donates an OH group
-water is eliminated
-petide bond is formed
-resulting molecule is a dipeptide
-

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11
Q

what is the primary structure

A

sequence of amino acids in the polypeptide chain

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12
Q

what is the secondary structure

A

the polypeptide chain doesn’t remain straight hydrogen bonds form between the amino acids in the chain, this makes sections of it to coil into an alpha helix of a beta pleated sheet

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13
Q

what is the tertiary structure

A

the coiled/folded chain of amino acids is often coiled an folded further
-more bonds form between the different points of the polypeptide chain
-hydrogen bonds, ionic , covalent(disulphide bridges) also form when two molecules of cysteine come close together
-the surfer atoms bond together
-final 3D structure of a proton made from the amino acid chain

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14
Q

what is the quaternary structure

A

-protein is made of more than one polypeptide chain , its the way that the different chains are arranged together,simlar bonds found in the tertiary structure are present here haemoglobin has a quaternary structure

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15
Q

how does a protein determine its function

A

by its shape

16
Q

what is one part of a molecule called

A

active site

16
Q

how is the activation energy lowered when a substrate fits into the active site

A

-holding substrate molecules close together and so that bonds can be made
-putting a strain on bonds in the substrate molecule and so they break more easily
-changing the substrate will successfully collide with the enzymes molecules

17
Q

what happens when you change the shape of the active site

A

stops the enzyme from working-denaturation

18
Q

what is the lock and key model

A

substrate fits into the active site like a key fits into a lock.They are complementary and so show specifically

18
Q

what is the induced fit model

A

the enzyme substrate complex changes shape slightly to accommodate the fit , this helps to explain why enzymes are so specific and only bond to one particular substrate
-the substrate needs to have the correctly shaped active site as well as making the active site change shape in the right way

19
Q

why is measuring initial rates of reaction important

A

as a reaction proceeds reactants are being used up , means the substrate is becoming less concentrated which will cause the reaction to slow down

19
Q

how do you test for proteins

A

-bieuret test
-solution needs to be alkaline so first add a few drops of sodium hydroxide solution
-add some copper sulphate solution
if protein is present the solution will turn purple, if not remains blue

20
Q

what are enzymes made out of

A

proteins

21
Q

what are enzymes

A

biological catalysts - speed up chemical reactions in cells

22
Q

what do enzymes act on

A

substrate molecules

22
Q

what is an active site

A

specific shape for the substrate to enter which forms a enzyme sublate complex

23
Q

are enzymes used up in reactions

A

no , can be produced in small amounts

24
Q

how do enzymes work

A
  • molecules in solution are continually moving around with kinetic energy
    -for reactions to take place molecules need to make successful collisions
    -the kinetic energy required for the reaction to take place is called the activation energy
    -enzymes lower the activation energy of a reaction
    -this means thatraection are able to take place at lower temp when enzymes are involved
    -increasing the temp when enzymes are involved , gives molecules more kinetic energy and so the rate of reaction will increase
    -increase the conc of the molecules also increase the rate of reaction
25
Q

how can temp effect enzyme activity

A

-rate of reaction increases with increased temp
-enzyme and sublate have more kinetic energy and collide more frequently
above a certain temp the enzymes vibrate a lot
-som of the bonds holding the enzyme molecule in shape begins to break
-the enzyme molecule loses its shape and actively - denatured

26
Q
A