Nucleotides And Enzymes Flashcards

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1
Q

Draw and label ATP

A
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2
Q

Draw and label a DNA nucleotide

A
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3
Q

State 2 differences between a DNA and RNA molecule

A

DNA has deoxyribose pentose sugar, whereas RNA has ribose DNA has thymine as a base, whereas RNA has Uracil

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4
Q

– Describe how a nucleotide is formed.

A

Base, pentose sugar and phosphate
Condensation reactions
Phosphoester bond between phosphate and sugar/carbon 5 of sugar and phosphate/carbon 1 on sugar and base 2 water molecules made

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5
Q

– What is the name of the bond that forms between nucelotides

A

phosphodiester

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6
Q

Describe how DNA replicates

A

Unwinding of helix by DNA helicase
Breaks H bonds between comp bases
Free nucleotides pair up with the complimentary bases
The free nucleotides bond with phosphodiester bonds
Due to DNA polymerase
Comp pairs form H bonds via DNA ligase

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7
Q

– Who discovered the structure of DNA

A

– Watson and Crick

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8
Q

– Who proved the semi conservative nature of DNA replication

A

Mehselson and Stahl

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9
Q

DNA strands run antiparallel – what does this mean?

A

One strand runs 5-3 whereas the other runs 3-5 direction

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10
Q

DNA polymerase can only work in one directionwhat direction is this

Why is that?

A

5-3
Only has a complimentary fit in that direction

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11
Q

What isotope of N was used as the primer

A

N15

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12
Q

after one set of replications, how many lines would show on the centrifuged test tube, and at what value

A

1 at 14.5

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13
Q

What enzymes work INSIDE cells

A

Intracellular

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14
Q

How do enzymes speed up the rate of reactions

A

bend bonds in the substrate, lower activation energy

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15
Q

How do you calculate the rate of an enzyme controlled reaction

A

(volume of product made/reactant used/time taken)

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16
Q

Why does increasing the temperature from 20 to 40 degrees usually speed up an enzyme controlled reaction.

A

Sub/enzyme molecules have more kinetic energy, more FScollions/more ESC formed,

17
Q

why does increasing the pH from 7 to 14 usually decrease the rate of reaction.

A

AS changes shape/denatured, no longer a comp fit, less ESC formed/less FSC

18
Q

How does an enzyme activator usually wor

A

changes shape of the active site, makes it more complimentary to substrate, more FSC/ESC form, increases reaction rate

19
Q

How does a non competitive inhibitor work

A
  • binds to allosteric site/non AS, changes shape of AS, less comp to substrate, less FSC/ESC formed.
20
Q

How does a competitive inhibitor work?

A

is similar shape to the substrate, so blocks active site/prevents substrate from bindings/ lowers formation of ESC

21
Q

Uses of ATP

A

muscle contraction, active transport, cell division, protein synthesis, DNA replication

22
Q

What are the purines

A

Guanine and Adenine

23
Q

What are the pyrimidines?

A

Cytosine thymine and uracil

24
Q

Structural differences between purines and pyrimidines

A

Purines have 2 rings
Pyrimidines have one

25
Q

Describe how nucleotides bond

A

phosphate of one nucleotide (hydroxile group) bonds with deoxyribose sugar (hydroxile group of carbon 3). DNA polymerase does this). Happens via a condensation reaction

26
Q

How are DNA strands separated

A

DNA helicase unwinds DNA, breaking H bonds between complimentary pairs.

27
Q

– Why should the initial rate of reaction be calculated when conducting enzymes controlled reaction?

A

As after this, some substrate will be used up, and then will become a limiting factor. Thus, the substrate concentration is no

28
Q

What may you need to draw on your graph to get the initial rate of reaction?

A

A tangent.

29
Q

whats the name of enzymes that work outside of cells

A

Extracellular

30
Q

Describe a primary protein

A

a sequence of amino acids bonded by peptide bonds in a straight chain

31
Q

Describe a secondary protein

A

folding of primary protein into alpha helix o beta pleated through hydrogen bonds

32
Q

Describe a tertiary protein

A

Folding of polypeptide chain into a more 3-D structure through ionic bonds, hydrophobic interactions or di-sulphide bonds on the R groups.

33
Q

Describe a quaternary protein

A

multiple polypeptide chains bonded together,