Macromolecules & enzymes (3&6) Flashcards

1
Q

monomer

A

small molecule which acts as a building block

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2
Q

polymer

A

large molecules made from same atoms but put together differently

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3
Q

isomers

A

molecules made from same atoms but put together differently

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4
Q

dehydration synthesis

A

linking 2 molecules by removing water

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5
Q

hydrolysis

A

breaking a molecule by inserting water

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6
Q

what are the 4 macromolecules

A
  1. carbohydrates
  2. nucleic acids
  3. lipids
  4. protiens
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7
Q

monosaccharides

A

simplest carbohydrates

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8
Q

disaccharides

A

2 monosaccharides linked by dehydration synthesis

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9
Q

polysaccharides

A

long chains of monosaccharides

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10
Q

nucleic acids

A
  1. phosphate
  2. nitrogen base (pyrimidines, purines)
  3. 5 carbon sugar
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11
Q

what are puries

A

adenine and guanine

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12
Q

pyrimidines

A

thymine, cytosine and uracil

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13
Q

how is dna and rna structured

A
  • 5->3
  • phosphodiester bonds
  • 2 nucleotides linked by dehydration synthesis
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14
Q

lipids

A
  • fats, oils, waxes, vitamins

- high proportion of c-h bonds

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15
Q

saturated fatty acids

A

have no c=c double bonds

high melting point bc regular shape

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16
Q

unsaturated fatty acids

A

1 or more c=c double bonds

irregular shape=low melting point

17
Q

phospholipids

A

1 glycerol
2 fatty acids-> non polar tails
1 phosphate group -> polar head

18
Q

phospholipid bilayer

A

polar (hydrophilic) head towards water
non polar (hydrophobic) tails away from water
-creates non polar barrier between 2 polar environments

19
Q

phospholipid bilayer

A

polar (hydrophilic) head towards water
non polar (hydrophobic) tails away from water
-creates non polar barrier between 2 polar environments

20
Q

what is primary structure

A

sequence of amino acids

21
Q

what is secondary structure

A

folding due to H-bonds

22
Q

what is tertiary structure

A

final folding of amino acid chain due to hydrophobic regions

23
Q

quarternary structure

A

multiple peptides

held together by H-bonds

24
Q

denaturation

A
loss of shape=loss of function
breaks due to
1. PH
2. Temp
3. Ionic concentration
25
chaperones
proteins that help others fold correctly | also can repair some others
26
endothermic
energy of products > reactants
27
exothermic
energy of reactants > products
28
anabolic
reaction that builds larger molecules
29
catabolic
reaction that breaks into smaller molecules
30
activation energy
energy required to start reaction
31
enzyme
biological catalyst
32
first law of thermodynamics
energy can not be created or distroyed
33
second law of thermodynamics
disorder (entropy) is always increasing - more ordered/less stable - less ordered/more stable
34
metabolism
total of all chemical reactions in an organism
35
how can you increase reaction rate
1. increse kinetic energy | 2. lower activation energy
36
active site
where substrates bind to an enzyme | - only specific substrate will bind
37
biochemical pathways
multiple reactions in a sequence | -without one, the proceeding can not work
38
feedback inhibition
- end product of pathway binds to an allosteric site on first enzyme - shut down pathway so raw materials and energy are not wasted.