proteins 1.6 Flashcards

(45 cards)

1
Q

what are proteins made of

A

amino acids

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2
Q

what does the sequence of DNA bases determine

A

the order of amino acids

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3
Q

what does the order of amino acids determine

A

the structure and function of the protein

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4
Q

name the 5 types of proteins

A

structural, enzymes, hormones, antibodies and receptors

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5
Q

describe structural proteins

A
  • they make up many essential components of the cell membrane and they help hold the structure of the cell membrane
  • examples of structural proteins are keratin that’s found in hair and nails and collagen found in skin, bones and tendons
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6
Q

describe enzymes

A
  • biological catalysts because they speed up chemical reactions in every living cell and they remain unchanged
  • because they remain unchanged they can be used over and over again without being used up
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7
Q

describe hormones

A
  • are chemical messengers released by glands in our bodies and travels in the bloodstream
  • they travel to somewhere else in the body act according their functions
  • involved in growth and metabolism
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8
Q

describe antibodies

A
  • y-shaped molecules that are made of lymphocytes that defend the body from disease
  • antibodies stay in our bodies so the next time our bodies come into contact with a specific pathogen it can respond fast
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9
Q

describe receptors

A

molecules which allow specific molecules to bind to them and receptors are found on the surface of cells and on the inside of cells

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10
Q

what is a chemical reaction

A

a process in which one or more substances is changed into one or more different substances

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11
Q

what is a product

A

the substances presence after the reaction takes place

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12
Q

what is activation energy

A

when chemical reactions need a certain amount of energy to take place

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13
Q

what produces enzymes

A

all livings cells

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14
Q

why are enzymes so important

A

because without enzymes chemical reactions within the body the reactions would be too slow to support life

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15
Q

how do enzymes work

A

they work by lowering the activation energy of the reaction so the reactions can take place at lower temperatures

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16
Q

how is the shape of the enzymes activation site determined

A

by the sequence and bonding of amino acids

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17
Q

the enzymes mechanism of action

A
  1. the specific substrate enters the enzymes active site
  2. the enzyme-substrate complex is formed and the substrate has enough energy for the reaction to take place
  3. the reaction takes place and the substrate turns into products
  4. the products are released from the enzyme and the enzyme remains unchanged
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18
Q

the 2 types of enzyme reactions

A

degrading reactions and synthesis reactions

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19
Q

describe degrading reactions

A

when one large substrate is broken down into two or more smaller products

20
Q

describe synthesis reactions

A

when two or more smaller substrates are built up into one large product

21
Q

what is digestion

A

the process in which the large molecules in food we eat are broken into smaller molecules and this allows them to be absorbed into the bloodstream

22
Q

examples of degrading reactions

A

SAM, PPP, Lipase and HPCOW

23
Q

example of synthesis reactions

24
Q

describe amylase

A

a digestive enzyme found mainly in our stomachs and saliva

25
what does amylase break starch into
it breaks down starch into maltose
26
describe pepsin
it breaks down protein and is found in the stomach
27
what does pepsin break protein into
breaks down protein into peptides
28
describe lipase
it breaks down fats
29
what does lipase break fats down into
fatty acids and glycerol
30
what does catalase break hydrogen peroxide into
oxygen and water
31
describe phosphorylase
it’s a synthesis enzyme and catalyses the synthesis of glucose-1-phosphate into starch
32
how do you determine if starch is present
test with iodine solution. it it stays a yellow/brown colour there’s no starch present but if the iodine solution turns a blue/black colour there’s starch present
33
the 3 types of experimental design
validity, reliability, controls
34
explain validity
- is to do with the “fairness” of the investigation | - in any experiment only one factor should be changed and all other variables should be kept the same
35
explain controls
- is identical to the original experiment in every way except that the factor that causes the change is removed - it is then replaced by something that doesn’t bring about change
36
explain reliability
to ensure reliability of the results and experiment, the experiment has to be repeated and several readings and sample have to be taken
37
what are the effects of temperature on enzymes
- at low temperatures the enzymes have very little energy and therefore do not collide often with substrate molecules - as the temperature increases, enzyme substrate molecules collide more often meaning that reaction rate increases
38
what is the optimum temperature
the temperature at which an enzyme is most active
39
describe denatured
when the increased temperature breaks the bonds holding the amino acids together - this causes the shape of the enzymes active site to be altered and the enzyme can’t bing to the substrate - the enzyme is now denatured and permanently inactive
40
when is amylase most active
pH 7
41
what is pepsin optimum pH
pH 2
42
what are enzymes made of
amino acids
43
what does it mean when it says enzymes are specific
the different enzymes have different shaped active sites that are complementary to the substrate that binds to them and each different enzyme acts on one substrate only
44
what is an active site
position on the surface of an enzyme molecule to which specific substrate molecules can bind
45
what is a substrate
the substance in which an enzyme acts upon