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AP Bio > Structure and Function -- Macrmolecules (more) > Flashcards

Structure and Function -- Macrmolecules (more) Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What are the macromolecules

A

carbs lipids nucleic acids proteinP

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2
Q

Macromolecules

A

super large molecules

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3
Q

Polymers

A

long molecule that consists of many smaller building blocks linked covalently

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4
Q

Monomers

A

the things that make up polymers
they can also have their own individual function

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5
Q

Enzyme

A

macromolecules that speed up chemical reactions

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6
Q

What are the names for the process of how macromolecules are formed/broken respectively

A

dehydration synthesis and hydrolysis

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7
Q

Hydro

A

water

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8
Q

Lyse

A

break apart or split

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9
Q

Hydrolysis aka

A

digestion

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10
Q

Sugars are made of what macromolecule

A

carbs

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11
Q

Monosaccharides are made of how many carbons

A

3-7

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12
Q

What is the shape of glucose when it is in water

A

ring

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13
Q

What is the shape of 5-6 carbon carbs when they are put in water

A

ring

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14
Q

Most sugars end in

A

ose

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15
Q

All carbs have what fxnal groups

A

carbonyl group and hydroxyl group

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16
Q

Sugars are classified by what

A

size

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17
Q

3 carbon sugar name

A

triose

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18
Q

5 carbon sugar name

A

pentose

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19
Q

6 carbon sugar name

A

hexose

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20
Q

example of hexoses

A

fructose and glucose

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21
Q

assymetric carbon

A

carbon that is attached to 4 different atoms or atom groups

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22
Q

Cellular respiration

A

cells extract energy from glucose molecules by breaking them down

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23
Q

The carbon skeletons of sugars can be used ot synthesize what other things

A

other organic molecules or poly or di sacchs

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24
Q

Disaccharide

A

2 monosaccharides joined by a glycosidic linkage

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25
Q

Glycosidic linkage

A

covalent bond formed between 2 monosacchardides by dehydration synthesis

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26
Q

Starch

A

polymer of glucose molecules that is stored in plastids which allows plants to stock a shit ton of glucose which can be hydrolyzed for energy

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27
Q

Plastid

A

organelles in cells used for storage

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28
Q

What is the shape of starch

A

helix – branch or unbranched

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29
Q

example of plastid

A

chloroplast

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30
Q

Glycogen

A

polysachharide or polymer of glucose where animals store energy and glucose

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31
Q

are carbs long or short term energy

A

short (usually depleted in 24 hours)

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32
Q

What is the shape of glycogen

A

helix branched

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33
Q

Where do vertebrates store glycogen

A

liver and muscle cellsC

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34
Q

Cellulose

A

structural polysaccharide; polymer of glucose

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35
Q

Shape of cellulose

A

long structural hydrocarbons that are straight and unbranched

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36
Q

What differentiates cellulose from other common polysaccharides

A

it has different glycosidic linkages bc the glucoses are upside down alternating unlike how theyre all the same for starch, glycogen, etc.

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37
Q

What is the reason that some organisms can digest glycogen but not cellulose

A

bc the glycosidic linkages are different so that the hydroxyl group is aternatively on the top or the bottom –> so most organisms dont have the correct enzymes so it js slides into the rest of their shit

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38
Q

Chitin

A

structural polysaccharide of arthropods that they use ot make exoskeletons –> its soft then its hard ;P so its strong structurally

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39
Q

Why are chitin and cellulose similar

A

they have the wonky glycosidic linkage different hing

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40
Q

example of an organism that uses chitin and how

A

fungi in its cell walls

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41
Q

Does fat have monomers

A

no

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42
Q

What is fat made of

A

glycerol and fatty acid

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43
Q

Glycerol is what type of molecule

A

alcohol

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44
Q

Fatty acid

A

a long carbon chain that is nonpolar and it makes the whole fat molecule hydrophobic

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45
Q

how long is a fatty acid chain

A

16 - 18 carbons

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46
Q

what fxnal group does fatty acid have

A

carboxyl acid

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47
Q

Fat aka

A

triacylglycerol or triglyceride

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48
Q

What bonds the fatty acid to the glycerol in a fat molecule

A

ester linkage

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49
Q

ester linkage

A

a bond formed by dehydration synthesis between they oxygen of the hydroxyl group of the glycerol and the carbon of the carboxyl group of the fatty acid

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50
Q

the double bonds in unsaturated fat are cis or trans

A

cis

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51
Q

Lipids

A

long term energy storage (better than carbs)

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52
Q

Do lipids have monomers

A

no

53
Q

Are lipids molecules

A

yes they even sometimes form macromolecules

54
Q

Structure of lipids

A

hydrocarbon

55
Q

Lipids polar or nonpolar

A

nonpolar

56
Q

Lipids hydrophobic or philic

A

phobic

57
Q

How many carbons is usually in lipids

A

usually 16-18

58
Q

Hydrogenated

A

bad, unsaturated fats that have been synthetically converted to saturated fats by adding hydrogen and trans fats

59
Q

Saturated Fat is bad why

A

bc it can cause atherosclerosis

59
Q

Atherosclerosis

A

clogged arteries

60
Q

Trans Fat

A

unsaturated bonds with trans double bonds ( H on opposite sides of the double bond)

60
Q

What do trans fats do to cholesterol

A

increase LDL and reduce HDL

60
Q

HDL

A

good cholesterol high density lipoprotein

61
Q

LDL

A

low density lipoprotein bad cholesterol

61
Q

Do trans fat occur in nature

A

yes

62
Q

Adipose Cells

A

cells where mammals store long term energy and does the organ cushioning

62
Q

What organisms have cholesterol in their cell membranes

A

animal cell membranes

62
Q

Main purposes of fat

A

energy
insulation
organ cushioning

63
Q

Phospholipid

A

like a fat molecule with only 2 fatty acid groups instead of 3 and the 3rd hydroxyl group is bonded to the phosphate group which is negatively charged
also usually there’s another polar or charged molecule that is linked to the phosphate group

64
Q

Phospholipid is important for what

A

cell membrane (phospholipid bilayer and in micelles)

65
Q

Are the heads of phospholipids hydrophilic or hydrophobic

A

hydrophilic

66
Q

Are the tails of phospholipids hydrophilic or hydrophobic

A

hydrophobic

67
Q

Why and how is the tail of a phospholipid bent

A

because there is a double bond so its unsaturated and the tails don’t freeze together

68
Q

Steroids

A

lipids that have a carbon skeleton of 4 fused rungs

69
Q

Examples of steroids

A

cholesterol and sex hormones

70
Q

Catalyst

A

chemical agents that speed up chemical reactions

71
Q

Amino Acid

A

organic molecule with amino group, carboxyl group, R group and H that has an assymetric carbon

72
Q

What makes amino acids different from each other

A

the r Group

73
Q

what is the R group aka

A

side chain

74
Q

Nonpolar amino acids are

A

hydrophobic

75
Q

Polar amino acids are

A

hydrophilic

76
Q

Basic amino acids have what

A

a positive R group

77
Q

Acidic amino acids have

A

negative side chain because of carboxyl group in ionized form

78
Q

Are acidic and basic amino acids hydrophobic or hydrophilic

A

hydrophylic because they are charged

79
Q

Peptide bond

A

covalent bond between the nitrogen of the amino group of one and the carbon of the carboxyl group of another

80
Q

What are the ends of 2 amino acids bonded together

A

amino group and a carboxyl group on the other end

81
Q

Polypeptide backbone

A

The non-R group of amino acid polymers, consisting literally of -N-C-C-N-C-C-N-

82
Q

Shape determines

A

function

83
Q

Do polypeptides = proteins

A

no because polypeptides can be proteins (single) but they have to be twisted and folded so polypeptides are just long primary structure

84
Q

Globular Proteins

A

proteins that are roughly spherical theyre rough and wide and theyre soluble in water

85
Q

Fibrous proteins

A

proteins shaped like long fibers; insoluble in water

86
Q

All proteins have what levels of structure

A

1-3

87
Q

Why do only some proteins have quartenary structure

A

because not all proteins consist of more than one polypeptide chain

88
Q

What are the protein structure levels

A

primary
secondary
tertiary
quaternary

89
Q

Primary protein structure level

A

sequence of amino acids which is determine by DNA

90
Q

If there were 127 amino acids in a chain how many different ways can you make the protein chain and why

A

20^127 because 20 amino acids exist in nature

91
Q

Secondary protein structure level

A

coil/fold due to hydrogen bonds between the H+ of amino group and O- of catboxyl group

92
Q

What is the coil called in secondary structure in protein structure levels

A

alpha helix

93
Q

What is the fold called in secondary structure in protein structure levels

A

beta pleated sheet

94
Q

Tertiary protein structure level

A

overall shape of a polypeptide which results from the interactions between the R-groups

95
Q

What are some examples of the tertiary bonds wjocj caise overall shapes of polypeptides

A

hydrophobic interaction
disulfide bridge

96
Q

Hydrophobic interaction

A

amino acids (nonpolar) end up in the middle and are held together by Van der Waals forces

also H bonds hold together

also bonds bwteen positive and negative

97
Q

Disulfide bridge

A

covalent bond between sulfurs of the sulfhydryl groups of 2 cysteines; super strong

98
Q

Quaternary

A

association of 2+ polypeptides

99
Q

Denaturation

A

proteins change shape because of wrong conditions because can disrupt bonds that hold it together

100
Q

What are some of the wrong conditions that can cause denaturation

A

wrong pH, temp, salt concentration, etc.

101
Q

Can denaturation be fixed?

A

yes if you put them back in the right conditions

102
Q

Chaperonins

A

proteins that encase other proteins-to-be so they are in the right conditions to fold

103
Q

Why are chaperonins important

A

because if proteins fold in the wrong conditions it could lead to fatal diseases such as CF, sickle cell disease, etc.

104
Q

When proteins-to-be go into chaperoning proteins what level of structure are they in

A

primary and they leave as secondary

105
Q

X-Ray Crystallography

A

shoot X-rays a crystallized and hardened protein and look at defraction patter ti assess design of protein

106
Q

Gene

A

a discrete unit of hereditary information consisiting of specific nucleotide sequences in DNA

107
Q

Gene expression

A

DNA directs RNA –> protein synthesis (in ribosomes)

108
Q

Polynucleotides

A

polymers of nucleic acids

109
Q

Nucleoside

A

nucleotide without phosphate

110
Q

Nucleoside aka

A

nucleoside monophosphate

111
Q

Pyrimidine

A

six carbon ring ( C, U, T)

112
Q

Purine

A

six carbon ring fused to a five carbon ring (G,A)

113
Q

Phosphodiester linkage

A

the covalent bond between nucleotides between the phosphate group of one and the sugar of another

114
Q

Where do the phosphodiester linkages appear

A

on the outside (ribbon part) of the double helix

115
Q

Where are the hydrogen bonds in DNA

A

between the bases (in the middle)

116
Q

Antiparallel

A

the 2 sugar-phosphate backbones are on the outside of the helix and they run in oppposite directions; one is 5’ -> 3’ and the other one is the other way

117
Q

RNA has how many strands

A

one

118
Q

DNA has how many strands

A

2 –> double helix

119
Q

If organisms have similar molecular geanologies…

A

they are more related

120
Q

What causes the polar head of a phospholipid

A

the top is negatively charged because of phosphate and the bottom is positevely charged because instead of a third fatty acid chain (like in a fat molecule) there is a choline which is positively charged

121
Q

Steriod purpose

A

chemical messengers/hormones

122
Q

What is in the backbone that is coiled/foiled in secondary protein structure

A

everything but the R-group

123
Q

What are the helix and the beta pleated sheet held together by

A

hydrogen bonds

AP Bio (66 decks)

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