chapter five Flashcards

structure and function of macromolecules

1
Q

polymers

A

large compounds made of many monomers

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2
Q

what are the four types of macromolecules?

A

carbs, proteins, lipids, nucleic acids

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3
Q

dehydration/condensation reaction

A

synthesizing a polymer, removes a water molecules forming a new bond

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4
Q

hydrolysis

A

breaking down a polymer, adds a water molecules breaking a bond

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5
Q

carbohydrates

A

fuel and building materials

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6
Q

what is the monomer of carbs?

A

monosaccharides

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7
Q

general formula of carbs?

A

C6H12O6

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8
Q

glucose typically forms what shape?

A

ring form with 3-7 carbons

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9
Q

disaccharide or two monosaccharides = ?

A

glycosidic linkage

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10
Q

glucose + glucose = ?

A

maltose

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11
Q

glucose + galactose = ?

A

lactose

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12
Q

glucose + fructose = ?

A

sucrose

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13
Q

dissacharide

A

quick burst of short lived energy

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14
Q

polysaccharides

A

energy storing, for day or two

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15
Q

starch

A

plants, stored in plastids

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16
Q

glycogen

A

animals, stored in muscles and liver

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17
Q

cellulose

A

found in plant cell wall (leaves), herbivores

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18
Q

chitin

A

more complex than cellulose, found in insects, spider, crab

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19
Q

lipids

A

energy storage and barriers

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20
Q

what is the monomer of lipids?

A

fatty acids

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21
Q

glycerol

A

alcohol with 3 C’s and OH group

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22
Q

hydrocarbon chain

A

nonpolar, lots of energy stored

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23
Q

lipids can store two times the energy as _____?

A

carbs

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24
Q

saturated fat

A

from animals, solid at room temperature, no C=C

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25
unsaturated fat
from plants, liquids or oils, one or more C=C
26
functions of lipids, specifically fats
cushioning around organs, insulation (blubber)
27
phospholipid bilayer
heads - polar, hydrophilic tails - nonpolar, hydrophobic
28
steroids
made of various functional groups
29
what is the backbone to steroids?
cholesterol
30
arteriosclerosis
build up plaque in arteries, heart attack
31
polypeptide chains
proteins are a chain of amino acids linked together by peptide bonds
32
what is the monomer of proteins?
amino acids
33
R group: amino group
basic, positively charged
34
R group: carboxyl group
acidic, negatively charged
35
nonpolar R groups
no O, hydrophobic
36
polar R groups
with -OH or just an = O, hydrophilic
37
peptide bond formation
condensation rxn, amino end is designated at beginning and carboxyl end is designated at end
38
protein conformation (shape)
normal, nature, typical shape
39
primary structure
chain of amino acids in order, DNA recipe, mutation
40
secondary structure
two types, caused by H bonding between amino acid and carboxyl groups: helix - coil pleated sheet - folded
41
tertiary structure
different amino acids = different R groups ionic bond - charged R groups disulfide bridge - S-S hydrogen bond - polar van der waals - non polar
42
quaternary structure
optional, 2 polypeptides join together to make protein, not all proteins have this level of structure
43
denatured
change native confirmation (hair)
44
sickle cell anemia
genetic change may cause protein shape change
45
nucleic acids
central dogma
46
DNA
stores and transmits coded info, determines amino acid sequences in proteins, nucleus (double stranded)
47
RNA
takes DNA's message out of the nucleus, forms ribosomes where proteins are made
48
what is the monomer of a nucleic acid?
nucleotide
49
ribose
RNA
50
deoxyribose
DNA
51
pyrimidines (1 ring)
cytosine thymine (DNA only) uracil (RNA only)
52
purines (2 rings)
adenine guanine
53
polymer formation
direction matters, 3' (OH) and 5' (P)
54
enzymes
proteins in the body that speed up a reaction
55
catalyst
anything that speeds up a reaction
56
activation energy
needed to start a reaction
57
transition state
unstable point where the reactants have absorbed enough energy to break and store to rearrange
58
substrate
reactant with enzyme
59
active site
area of enzyme that binds to substrate
60
induced fit
enzyme changes shape after binding, ex: handshake
61
temp and pH
rate can increase or decrease, disrupts H- bonds and denatures proteins and enzymes
62
cofactors
non protein helpers
63
coenzymes
organic cofactors
64
competitive inhibitiors
compete with substrate for active site
65
noncompetitive inhibitors
molecule binds to a different area on enzyme and change its shape
66
feedback inhibition
metabolic pathway is stopped when the product binds to the enzyme and inhibits activity
67
localizing
specific enzymes for specific jobs