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Biology > Nucleic Acids / Enzymes > Flashcards

Nucleic Acids / Enzymes Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What does DNA stand for

A

Deoxyribose nuclei acid

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2
Q

Describe genes

A

Small sections of chromosomes

Code for for different characteristics

Inherited

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3
Q

AT and GC are called

A

Complimentary base pairs

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4
Q

A change in one base is enough to

A

Change the structure of the protein and disrupts how it works

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5
Q

What two bases go together

A

Adenine +thymine

Cytosine + guanine

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6
Q

What are the two types of nucleic acids

A

DNA

RNA

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7
Q

What are the three types of RNA

A

mRNA
tRNA
rRNA

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8
Q

What monomer makes up nucleic acids

A

Nucleotides

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9
Q

What does RNA do

A

Read and translate information for protein synthesis

Genetic code exists out the nucleus

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10
Q

What does DNA do

A

Stores information

Found in nucleus

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11
Q

Nucleotides are made of what 3 units

A

Phosphate group

5 carbon sugar (pentose )

Organic nitrogenous base (ATGC)

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12
Q

The base and sugar join with a ? Bond

A

Glycosidic

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13
Q

The phosphate and sugar ion with a ? Bond

A

Phosphodiester

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14
Q

Glycosidic and phosphodiester bonds both require a ? Reaction to occur

A

Condensation

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15
Q

Describe purines

A

Double ringed structures

Adenine and guanine

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16
Q

Describe pyrimidines

A

Single ringed structures

Thymine and cytosine

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17
Q

What is a monomer

A

Molecules that when separated make up polymers

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18
Q

What is semi conservation replication

A

1/2 of the original DNA strand is conserved

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19
Q

What’s the anti parallel sugar phosphate back bone

A

Runs in opposite directions

5 3

3 5

Carbon prime ends

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20
Q

Hydrogen bonding between complementary bases form rungs stabilise the

A

Structure

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21
Q

Why must DNA be stable

A

Otherwise the code (instructions ) could go wrong

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22
Q

How does DNA replicate

A
  • DNA unwinds
  • enzyme helicase unzips the double helix
  • parent stands act as a template
  • free floating nucleotides join firm the cytoplasm
  • they join to the exposed complementary base pairs (AT-GC)
  • hydrogen bonds form
  • sugar phosphate backbone forms
  • each new molecule has 1 old and 1 new strand
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23
Q

Describe lagging strand

A

New strands synthesised in short sections, then joins together

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24
Q

Describe leading strands

A

Synthesised in one continuous length

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25
Q

DNA needs to be replicated for

A

Growth

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26
Q

What is RNA

A

A template of DNA

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27
Q

How does RNA and DNA differ

A

Ribose is smaller and shorter

The nucleotides contain ribose sugar where as DNA contain deoxyribose

RNA- the nitrogenous base uracil instead of thymine - U is complimentary to A

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28
Q

What is transcription

A

The process by which DNA is read to produce a stand of mRNA

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29
Q

What’s the transcription process

A
  • the gene unwinds and unzips
  • hydrogen bonds between complementary nucleotide bases break
  • RNA polymerase catalyses the formation of temporary hydrogen bonds between RNA nucleotides and their complementary unpaired DNA bases- A+T, C+G ,G+C, U+A, TEMPLATE STARND
  • A length of RNA that is complementary to the template strand of the gene is produced . it is therefore a copy of the other DNA starnd, the coding strand
  • the mRNA now passes out the nucleus ,through the nuclear envelope and attaches to ribosomes
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30
Q

What is translation

A

formation of a protein, at ribosomes , by assembling amino acids into a particular sequence according to the coded instructions carried from DNA to the ribosomes by mRNA

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31
Q

What are enzymes

A

They’re made of protein , so they are made inside ribosomes

32
Q

If the base sequence is wrong , what happens

Enzymes

A

Mutation

The recipe is wrong so the enzyme won’t have its amino acid in the right order

Won’t work properly

33
Q

DNA determines the sequence of

A

Amino acids

34
Q

The sequence of amino acids in the enzyme determines its final shape , called the ? Structure

A

Tertiary

35
Q

Enzymes are

A

Soluble in water

Globular

36
Q

Enzymes are biological catalysts , what are biological catalysts

A

Thy speed up metabolic reactions but aren’t altered by them

37
Q

What factors can effect enzymes

A

Temperature

PH

38
Q

How fast an enzyme works is called

A

Turn over rate

39
Q

Catalase can convert ? Hydrogen peroxide molecules per second to water and oxygen

A

6,000,000

40
Q

Examples of enzymes

A

Catalase

Amylase pepsin

41
Q

Describe catalase

A

Found in nearly all organisms exposed to oxygen

It breaks down harmful hydrogen peroxide into oxygen and water

Intracellular

42
Q

Describe anabolic

A

Process - binds prod us together

43
Q

Describe catabolic

A

Process - breaking products

44
Q

What is extracellular

A

Outside of the cell

45
Q

What is intracellular

A

Inside the cell

46
Q

Adding an enzyme reduces the

A

Amount of activation energy required for the reaction to take place

47
Q

Describe the lock and key mechanisms

A

The enzyme splits the substrate molecule into two smaller products . Enzymes can catalyse the reverse reactions

Substrate fits into the active site

48
Q

Describe the induced fit model

A

The two substrates don’t quite fit until the enzyme engulfs the substrate abut

49
Q

What is the rate of reaction

A

The speed at which the reactant or Substate is changed into a product

50
Q

How can you monitor the rate of reaction

A

By measuring how fat the product is made by or product disappear

51
Q

Describes the initial rate of reaction

A

When a reaction happens , substrate gets used up and Product gets formed. As this process the enzyme had less Substate to work on . So it’s rate slows down

52
Q

What is a limiting factor

A

Is one that can alter the rate of a reaction if all factors are kept constant

53
Q

Heating enzymes increase

A

Kinetic energy of Substate and enzyme molecules leading to an increased frequency of random collisions

54
Q

More collisions of enzymes means

A

Higher reaction rates

55
Q

How heating affects molecules

A

Also vibrates molecules , this creates weaker binds which hold the tertiary structure together . Can be broken . This changes the shape of the enzyme and its active site . The Substate no longer fits

56
Q

Acidic=

Neutral =

Basic =

A

0
7
14

57
Q

What does PH mean

A

The amount of H+ ions

58
Q

How does PH affect enzymes

A

Their charge interferes with the ionic and hydrogen binds which hold their tertiary structure together . This changes their shape of enzymes and active site. Binding of Substate is compromised

59
Q

Extreme PH can lead to

A

Denature

60
Q

Optimum PH leads to

A

Maximum rate of reaction

61
Q

Describe cofactors

A

Molecules that increase the rate of reaction

Not proteins , they help proteins

Example iron and zinc

62
Q

Describe coenzymes

A

Organic molecules

Binds to enzymes and help them function

Contain carbon

Derived from vitamins

Sit at active site

Shuttle chemical groups from one enzyme to another

63
Q

Describe prosthetic groups

A

Cofactors that bond tightly to proteins or enzymes

Can be organic or metal and attach to proteins by covalent bonds

Can bind to proteins other than enzymes

Permanent bond

64
Q

How can you control the rate

A

Changes the amount of enzymes

Change the amount is Substate

Change the PH

Change the temperature

65
Q

Name the two inhibitors

A

Reversible

Irreversible

66
Q

Describe reversible inhibitors

A

His type is inhibitor can increase and decrease

67
Q

Describe irreversible / permanent inhibitors

A

This will stop the enzyme working forever

68
Q

What are the two types of reversible inhibitors

A

Competitive

Non competitive

69
Q

Describe competitive inhibitors

A

A substance competes with the substrate for the active site concentration of substrate and inhibitors are important

70
Q

Explain non competing inhibitors

A

not compete with the Substate for the active site

Only concentration of the inhibitor is important

71
Q

Describe end product inhibition

A

After catalysed reactions has reached completion , product molecules may stay tightly bound to the enzyme . Enzymes cannot form more products

72
Q

Describe metabolic sequences

A

Involves a series of enzymes catalysed reactions

The product of one enzyme becomes the Substate for the next enzyme catalysed reaction in the metabolic pathways

73
Q

Describe how snake venom works

A

Acts as a competing inhibitor preventing the acetylcholine from being broken down by acetycholinestrerase after impulse transmissions. This stops nerve impulses from being transmitted and stops muscles contractions causing paralysis

74
Q

Examples of no competitive inhibitors

A

Copper sulphate / catalase

75
Q

Examples of competitive inhibitors

A

Snake venom

76
Q

Describe the non competitive inhibitor process

A
  • the inhibitor enters the enzymes environment
  • the shape of the inhibitor is different to the shape of the Substate
  • the shape of the inhibitor does however match with a different part of the enzyme
  • this part is called the allosteric site
  • the inhibitor binds with site causing the reaction to occur which alters the enzymes tertiary structure
  • the enzyme Substate can no longer fit into the active site
  • if the inhibitor is reversible it can dissociate with the enzyme allowing the enzyme to regain its tertiary structure
77
Q

Competitive inhibitor process

A
  • due to kinetic energy all of the molecules are moving around
  • the inhibitor enters the enzyme environment
  • sometimes an inhibitor arrives at an active site before a Substate
  • the shape on the inhibitor matches with the shape of the Substate
  • other enzymes active sites are available to a reaction can still occur but just at a slow rate
  • the inhibitor binds with the enzyme active site , preventing a Substate from binding
  • if the amount of inhibitor were to increase this would slow down the rate further

Biology (10 decks)

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