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AP Biology > Unit 1 - Chemistry of Life > Flashcards

Unit 1 - Chemistry of Life Flashcards

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1
Q

what does all life on earth have in common?

A

made up of organic molecules

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2
Q

ionic bonding

A

bond in which an element transfers an electron to another element
- this results in ions

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3
Q

cations

A

positive ions

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4
Q

anions

A

negative ions

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5
Q

covalent bonding

A

a bond that involves the sharing of electrons

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6
Q

what does covalent bonding result in

A

stable configurations

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7
Q

nonpolar covalent bonds

A
  • electrons are shared equally
  • hydrophobic
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8
Q

electronegativity

A

when an atom is considered “electronegative”, it means it is one with a strong pull on electrons towards its nucleus
- results in partial charges

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9
Q

polar covalent bonds

A
  • one atom pulls electrons towards its nucleus
  • hydrophilic

ex: H2O

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10
Q

how do we know if a molecule is polar?

A
  • P, O, N, S, etc. cause that region of the molecule to be polar (hydrophilic) due to the high EN of those elements
  • N (nitrogen) means polar and basic
  • once you see charges, you know its polar
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11
Q

explain the covalent bonding in water

A
  • oxygen, which is highly electronegative, pulls on the hydrogens electrons
  • the bonds between the H and O within the molecule are POLAR COVALENT BONDS
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12
Q

how do we know if a molecule is nonpolar?

A
  • long chains of carbons and ringed carbon structures are nonpolar (hydrophobic)
  • symmetrical compounds are nonpolar
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13
Q

hydrogen bonds

A
  • a WEAK attraction between a hydrogen atom and a highly electronegative atom (ex: H2O)
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14
Q

hydrophilic

A
  • mix with water
  • polar
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15
Q

hydrophobic

A
  • will NOT mix with water
  • nonpolar
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16
Q

water’s 7 properties

A
  1. cohesion
  2. adhesion
  3. high heat capacity + heat of vaporization
  4. transpiration
  5. surface tension
  6. liquid water vs ice
  7. water as a solvent
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17
Q

cohesion

A
  • waters ability to stick to itself
  • due to hydrogen bonding
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18
Q

adhesion

A
  • water’s ability to stick to polar molecules
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19
Q

heat capacity

A
  • the amount of energy needed to change the temperature of water
  • water has a high heat capacity

**this is why organisms can live in aquatic environments

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20
Q

heat of vaporization

A

**thermoregulation
- water, in the form of sweat, will absorb heat energy
- this reduces body temperature

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21
Q

transpiration

A

evaporation of water through the leaves of a plant
- water will stick together (cohesion) and stick to the xylem (adhesion)
- this prevents the backflow of water
- pulled up the plant as water evaporates from the leaves

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22
Q

surface tension

A
  • intermolecular forces at the top are stronger than below
  • extreme due to cohesion and adhesion forces; why certain insects can walk on water bc the interaction btw their bodies and water is weaker than the Hydrogen bonds between H2O
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23
Q

liquid water vs ice

A

ice is less dense than H2O therefore ice floats and aquatic organisms can survive in the cold

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24
Q

water as a solvent

A

water will dissolve ionic and polar compounds

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25
Q

carbon

A
  • has 4 valence electrons
    - forms 4 covalent bonds with other elements which causes diff molecular shapes
  • found in ALL organic compounds
  • used to make macromolecules
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26
Q

4 major organic molecules (macromolecules)

A
  • carbohydrates
  • lipids
  • amino acids / proteins
  • nucleic acids
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27
Q

carbohydrates

A
  • polar
  • made up of C, H, O
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28
Q

function of carbohydrates

A
  • energy
  • makes up the cell walls of plants and prokaryotes
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29
Q

lipids

A
  • nonpolar
  • made up of C, H, O
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30
Q

function of lipids

A
  • energy source
  • make up the cell membrane
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31
Q

amino acids / proteins

A
  • polar
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32
Q

nucleic acids

A
  • polar
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33
Q

monomers

A

single molecule

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34
Q

polymers

A

many molecules put together

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35
Q

how are monomers and polymers synthesized?

A
  • dehydration synthesis
  • hydrolysis
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36
Q

dehydration synthesis

A
  • linking monomers together to form polymers
  • H2O is removed
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37
Q

hydrolysis

A
  • adding H2O to break polymers into monomers
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38
Q

hydroxyl

A
  • polar
  • “OH”
  • alcohol
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39
Q

carboxyl

A
  • polar
  • “COOH”
  • carboxylic acids
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40
Q

phosphate

A
  • polar
  • organic phosphates
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41
Q

carbonyl

A
  • polar
  • think ketones and aldehydes!!
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42
Q

amino

A
  • polar
  • amines
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43
Q

sulfhydryl

A
  • polar
  • “-SH”
  • thiols
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44
Q

methyl

A
  • nonpolar
  • “CH3”
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45
Q

what is the importance of functional groups

A

they influence how molecules behave in reactions and with H2O

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46
Q

description of carbohydrates

A
  • C, H, O
  • the monomer is known as monosaccharide
  • drawn as hexagon, number 1-6 starting from right middle
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47
Q

monosaccharides

A

ex: glucose, fructose, galactose

ex: deoxyribose, ribose

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48
Q

hexose sugars

A
  • glucose, fructose, galactose
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49
Q

pentose sugars

A
  • deoxyribose, ribose
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50
Q

alpha glucose

A
  • the 2 hydroxyl groups (OH) are faced down
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51
Q

beta glucose

A
  • the left hydroxyl (OH) is faced down while the right is faced up
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52
Q

what is the difference between alpha glucose and beta glucose

A

the position of the hydroxyl (OH)

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53
Q

disaccharides

A
  • 2 monosaccharides linked together (via dehydration synthesis)
  • glucose + glucose -> maltose
  • glucose + fructose -> sucrose
  • glucose + galactose -> lactose
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54
Q

maltose

A
  • disaccharide
  • glucose + glucose -> maltose
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55
Q

sucrose

A
  • disaccharide
  • glucose + fructose -> sucrose
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56
Q

lactose

A
  • disaccharide
  • glucose + galactose -> lactose
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57
Q

glycosidic bonds

A

bond that links carbohydrates

58
Q

polysaccarides

A
  • starch
  • cellulose
  • glycogen
  • chitin
59
Q

starch

A

stored sugar in plants

60
Q

chitin

A

makes up the exoskeleton of insects

61
Q

glycogen

A

stored sugar in mammals

62
Q

cellulose

A
  • (fiber)
  • makes up the cell walls of plant cells
  • made up of beta glucose molecules which we CANNOT digest (we lack the proper enzymes)
63
Q

function of carbs

A
  • major energy source
  • make up cell walls
64
Q

elements of lipids

A
  • C, H, O
65
Q

are lipids polar/nonpolar generally?

A

they are nonpolar, hydrophobic (phospholipids are both)

66
Q

triglycerides

A
  • formed by combining a glycerol molecule (3 C sugar) and 3 fatty acids
  • saturated vs unsaturated fatty acids
67
Q

saturated fatty acids

A
  • saturated fats: no double bonds, solid at room temperature
68
Q

unsaturated fatty acids

A
  • unsaturated fats: 1 or more double bonds, “liquid at room temp”
  • nonpolar, hydrophobic
69
Q

what type of bonds are in triglycerides

A

ester bonds

70
Q

ester bond

A

links a glycerol and 3 fatty acids

71
Q

trans fats

A
  • stay straight so it can stack, unhealthy
72
Q

phospholipids

A
  • made up of a phosphate group (head), glycerol (3 C sugar), 2 fatty acids (tails)
  • the head is polar, tail is nonpolar
  • make up the cell membrane (phospholipid bilayer)
73
Q

amphipathic

A
  • contains both polar and nonpolar regions
74
Q

why are the tails of a phospholipid drawn differently

A

they are drawn differently to show saturated (straight) and unsaturated (squiggle)

75
Q

sterols/steroids

A
  • 4 fused carbon rings with attached functional groups
  • found in cell membranes (cholesterol) & signaling molecules/hormones ( testosterone, estrogen )
76
Q

functions of lipids

A
  • protection (of organs)
  • temperature regulation/insulation
  • **makes up the cell membrane
  • **can be used for energy
77
Q

protein’s elements

A

C, H, O, N and sometimes S

78
Q

protein’s monomer

A

amino acid

79
Q

protein’s polymer

A

polypeptide

80
Q

protein’s bond

A

peptide bond

81
Q

what determines proteins function

A

the shape

82
Q

amino acids - buffer

A
  • amino acid is a buffer (regulates pH)
  • buffer can accept/donate hydrogen
  • contains a variable side chain which is responsible for the properties of polypeptides
83
Q

primary structure of protein

A
  • the sequence of amino acids (coded for by DNA)
  • amino acid has directionality; from the n-terminus to c-terminus
  • peptide bonds
84
Q

secondary structure of protein

A
  • 2 types of folding: alpha helix and beta pleated sheet
  • **the structure is formed from the hydrogen bonding of the polypeptide backbone
85
Q

tertiary structure of protein

A
  • 3D structure when alpha helixes & beta sheets fold further due to r-group interactions
  • folds are due to the R-group interactions
  • hydrogen bonding
  • ionic bonds
  • covalent bonds “S-S” -> disulfide bonds, very strong
  • hydrophobic and hydrophilic interactions
86
Q

how do R-group properties determine how a protein folds?

A
  • hydrogen bonds -> hydrophobic vs hydrophilic
  • hydrophobic will tend to come inwards
87
Q

quaternary structure

A
  • 2 or more polypeptides combined
88
Q

protein functions

A
  • make up the muscles
  • antigens, antibodies
  • involved in transport; receptors
  • CTFR (cystic fibrosis)
  • enzymes (catalysts - speed up chemical rxns)
89
Q

mutations in proteins

A
  • DNA codes for the production of proteins
  • a change in the DNA can lead to a change in an amino acid -> changes R-group interactions
90
Q

what causes the partial charges in H2O

A
  • oxygen is more EN, therefore it has a stronger pull on the shared electrons w hydrogen
  • causes O to have partial “-“
  • causes H to have partial “+”
  • this uneven distribution of charge causes H2O to be polar
91
Q

what is the universal solvent

A

water

92
Q

what are waters properties attributed to

A

its polarity and ability to form hydrogen bonds

93
Q

hydrogen bonds: boils

A
  • when water boils, hydrogen bonds are breaking to cause H2O molecules to move rapidly (high specific heat)
94
Q

hydrogen bonds: freezes

A
  • when water freezes, H2O molecules get pushed apart therefore less dense; ice floats on water
95
Q

metabolism

A
  • sum of all chemical reactions that take place within an organism
  • catabolic: bond breaking
  • anabolic: bond forming
96
Q

proteins

A
  • they are polymers formed from amino acid monomers
97
Q

amino acids

A
  • made up of one central carbon covalently bonded to 4 things: hydrogen, acidic carboxyl groups, amino group, “R group”
98
Q

what gives amino acids their unique properties

A

the r-group which subs for different side chains that give amino acids their unique chemical properties

99
Q

when amino acids link together, what happens

A

dehydration synthesis occurs between amino group and carboxyl group
- known as a peptide bond

100
Q

polypeptide chains

A

primary structure of proteins which is formed during the process of translation at the ribosome

101
Q

protein stuctures

A

there are 4 levels of structure as it bends and folds upon itself; one wrong amino acid and folding will be incorrect

102
Q

the structure of each protein is dependent on

A
  • the chemical properties of the R-group & can be influenced by envi. factors

ex: R-group side chains that are hydrophobic will face inwards, away from aqueous environment

103
Q

carbohydrates: H to O ratio

A

always 2:1

104
Q

main difference in polysaccarides

A
  • glycosidic linkages, branching patterns, and functions
  • glucose, fructose, and galactose are isomers!!
105
Q

starch and glycogen linkage + monomer

A
  • monomer: alpha glucose
  • linkage: 1-4 alpha glycosidic linkage
106
Q

cellulose monomer + linkage

A
  • monomer: beta glucose
  • linkage: 1-4 beta glycosidic linkage
107
Q

lipids

A

diverse group of hydrophobic molecules that are nonpolar due to their hydrocarbon chains`

108
Q

lipids: H to O ratio

A
  • much larger than carbohydrate’s ratio (fewer O)
109
Q

fats / triglycerides

A
  • made up of glycerol molecule and 3 fatty acids held together by ester bonds
110
Q

types of proteins

A
  • globular proteins
  • fibrous proteins
111
Q

globular proteins

A
  • the do”ers”
  • carry out chemical reactions
  • ex: enzymes
112
Q

fibrous proteins

A
  • provide structural support
  • ex: collagen, cytoskeleton components
113
Q

do enzymes change during the chemical reaction?

A

no

114
Q

enzyme

A

catalyst; speeds up chemical reaction

115
Q

substrate

A

what the enzyme “works” on/binds to

116
Q

enzyme substrate complex

A

substrate bound to enzymes active site

117
Q

active site

A

where the substrate binds to the enzyme

118
Q

lock and key

A

specific substrate shape fits into ONE specific enzyme

119
Q

induced fit

A

enzyme changes shape to fit substrate

120
Q

competitive inhabition

A
  • a molecule that’s similarly shaped to the substrate fits into the active site of enzyme and blocks the substrate
121
Q

allosteric inhabition

A
  • allosteric receptor away from the active site
  • inhibitor binds -> the enzyme active site changes shape. substrate cannot bind
  • “non competitive inhibition”
122
Q

what factors affect enzyme activity

A
  • temperature
  • pH
  • substrate or enzyme concentration
123
Q

how does temperature affect enzyme activity

A
  • as temperature increases, enzyme activity increases to optimal temperature; then, enzyme activity decreases
  • the enzyme denatures: bonds start to break in tertiary and secondary structure
124
Q

**as long as primary structure is not altered

A

the polypeptide could be restored

125
Q

how does pH affect enzyme activity?

A
  • pH is a measure of how acidic or basic something is
126
Q

enzyme/substrate concentration effect on enzyme activity

A
  • as substance concentration increases, enzyme activity increases and then levels off
127
Q

function of nucleic acids

A
  • stores hereditary information (this is the code for proteins)
  • transmit hereditary information (express the protein)
  • “codes for the production of proteins”
128
Q

elements of nucleic acids

A
  • C, H, O, N, P
129
Q

monomer of nucleic acids

A
  • nucleotides
130
Q

polymer of nucleic acids

A
  • nucleic acid, DNA, RNA
131
Q

nucleotide composition

A
  • phosphate group; “-“ charge
  • pentose sugar
  • nitrogenous base
  • phophodiester bonds link nucleotides together
132
Q

phophodiester bonds

A
  • covalent
  • link nucleotides together
133
Q

pyrimidine

A
  • C, T; cytosine and thymine
  • shorter structure
134
Q

purine

A
  • A, G; adenine and guanine
  • longer structure
135
Q

what are pyrimidine and purine subgroups of

A
  • these are nitrogenous bases that make up different nucleotides in DNA and RNA
136
Q

DNA

A
  • double stranded
  • thymine
  • deoxyribose
  • antiparallel
137
Q

RNA

A
  • single stranded
  • uracil
  • ribose sugar
138
Q

what do DNA and RNA have in common

A
  • sugar phosphate backbone
  • 5’ -> 3’
  • both are made up of nucleotides
139
Q

complementary base pairing and bonding: A-T

A
  • Adenine and Thymine = 2 Hydrogen Bonds
140
Q

complementary base pairing and bonding: C-G

A
  • Cytosine and Guanine = 3 Hydrogen Bonds
141
Q

DNA is antiparallel

A
  • DNA always runs 5’ -> 3’; it has a 5’ end and 3’ end
142
Q

central dogma: DNA

A
  • DNA is going to transcribe itself into mRNA -> proteins
  • DNA codes for the production of proteins

AP Biology (1 decks)

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