3.1.4 proteins Flashcards

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1
Q

what are the monomers of proteins?

A

amino acids

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2
Q

what does the structure of an amino acid contain ?

A

amine group ( NH3)
carboxyl group (COOH)
R group (variable group)

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3
Q

what bond is formed from the condensation reaction between 2 amino acids?

A

peptide bond

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4
Q

how are dipeptides formed?

A

the condensation of two amino acids

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5
Q

how are polypeptides formed?

A

by the condensation of many amino acids

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6
Q

define primary structure of a protein

A

sequence of a chain of amino acids

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7
Q

define secondary structure of a protein

A

occurs when the sequence of amino acids are linked by hydrogen bonds and pleated sheets

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8
Q

define tertiary structure of a protein

A

occurs when certain attractions are present between alpha helices and pleated sheets

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9
Q

define quaternary structure of proteins

A

a protein consisting of more than one amino acid
may also contain a prosthetic group

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10
Q

how are disulphide bridges formed?

A

the amino acid cysteine contains sulfur atoms which can form disulphide bridges which are strong covalent bonds

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11
Q

how are ionic bonds formed?

A

formed between carboxyl and amine groups not involved in peptide bonds, or between oppositely charged R groups of amino acids

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12
Q

outline the biuret test

A

treat the sample with sodium or potassium hydroxide to make it alkaline
add a few drops of copper sulfate to the sample
a colour change from blue to lilac/ purple indicates the presence of a protein

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13
Q

outline the induced fit model of enzyme action

A

enzymes active site changes shape slightly to fit around the substrate
active site moulds around the substrate putting a strain on certain bonds in the substrate
this lowers the activation energy needed to break bonds
active site and substrate are not complementary

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14
Q

what factors affect enzyme activity?

A

temperature
PH
substrate conc.
enzyme conc.
inhibitors

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15
Q

explain the effect of temperature on enzyme activity

A

as temperature increases the kinetic energy of the enzyme and the substrate increases
this means there are more collisions between the active site of the enzyme and the substrate
this means there are more enzyme substrate complexes formed and more product

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16
Q

define PH

A

a measure of the concentration of hydrogen ions in a solution

17
Q

how do you calculate PH?

A

-log[H+]

18
Q

explain the effect of changing substrate concentration on enzyme activity

A

more substrate molecules bind to active sites and so more enzyme substrate complexes form
more product produced
once all active sites are in use the enzyme is saturated

19
Q

explain the effect of changing enzyme concentration on the enzyme activity

A

more enzyme active sites are available to bind to substrates meaning more enzyme substrate complexes formed and more product is released

20
Q

what is a competitive inhibitor?

A

a substance that binds at the active site of an enzyme

21
Q

what is a non-competitive inhibitor?

A

a substance that binds to the allostearic site of an enzyme

22
Q

what does optimum temperature mean for enzymes?

A

the temperature the enzymes work best at