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biology unit 1 > proteins 1.6 > Flashcards

proteins 1.6 Flashcards

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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

A

GPS

24
Q

describe amylase

A

a digestive enzyme found mainly in our stomachs and saliva

25
Q

what does amylase break starch into

A

it breaks down starch into maltose

26
Q

describe pepsin

A

it breaks down protein and is found in the stomach

27
Q

what does pepsin break protein into

A

breaks down protein into peptides

28
Q

describe lipase

A

it breaks down fats

29
Q

what does lipase break fats down into

A

fatty acids and glycerol

30
Q

what does catalase break hydrogen peroxide into

A

oxygen and water

31
Q

describe phosphorylase

A

it’s a synthesis enzyme and catalyses the synthesis of glucose-1-phosphate into starch

32
Q

how do you determine if starch is present

A

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
Q

the 3 types of experimental design

A

validity, reliability, controls

34
Q

explain validity

A
  • 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
Q

explain controls

A
  • 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
Q

explain reliability

A

to ensure reliability of the results and experiment, the experiment has to be repeated and several readings and sample have to be taken

37
Q

what are the effects of temperature on enzymes

A
  • 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
Q

what is the optimum temperature

A

the temperature at which an enzyme is most active

39
Q

describe denatured

A

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
Q

when is amylase most active

A

pH 7

41
Q

what is pepsin optimum pH

A

pH 2

42
Q

what are enzymes made of

A

amino acids

43
Q

what does it mean when it says enzymes are specific

A

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
Q

what is an active site

A

position on the surface of an enzyme molecule to which specific substrate molecules can bind

45
Q

what is a substrate

A

the substance in which an enzyme acts upon

biology unit 1 (6 decks)

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