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AP Biology > Chapter 2: Inorganic and Organic Chemistry > Flashcards

Chapter 2: Inorganic and Organic Chemistry Flashcards

1
Q

ion

A

a charged atom

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2
Q

ionization

A

the formation of ions by loss of electrons

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3
Q

Lewis Dot notation

A

a form of electron notation that involves only drawing the valence electrons

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4
Q

isotope

A

an atom that has a different number of neutrons than other atoms with the same atomic number

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5
Q

radioisotopes

A

radioactive isotopes

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6
Q

atomic mass

A

the number of neutrons plus the number of protons

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7
Q

Van Der Waal’s interactions

A

weak interactions between regions of nonpolar molecules, resulting from charge fluctuations within molecules

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9
Q

electronegativity

A

the measure of an atom’s tendency to hold or gain electrons

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10
Q

electrostatics

A

describes the tendency for positive and negative charges to attract

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11
Q

ionic bonds

A

form from the attraction of the oppositely charged ions

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12
Q

covalent bonds

A

form when the differences between the electronegativities of atoms are equal or similar

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13
Q

polar covalent bonds

A

result when one atom in a covalent bond is more electronegative than the other

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14
Q

hydrogen bonds

A

form from interactions between a partially positive hydrogen in one molecule and a partially negative atom (usually oxygen or nitrogen) in another molecule

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15
Q

solvent

A

a fluid in which molecules dissolve

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16
Q

dissociation

A

the breaking apart of molecules

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17
Q

specific heat

A

the amount of heat needed to raise the temperature of one gram by one degree Celsius

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18
Q

solubility

A

a substance’s ability to dissolve other substances

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19
Q

hydration shells

A

the result of separating ions from each other in a water molecule

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20
Q

adhesion

A

the property of water to cling to other materials because of its ability to form hydrogen-bonds

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21
Q

cohesion

A

the property of water to cling to other water molecules because of its ability to form hydrogen-bonds

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22
Q

surface tension

A

the result of cohesion, where a net force that acts on water molecules on the surface forms a “film” of tightly packed molecules

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23
Q

turnover

A

the process of water on the surface sinking as it approaches 4 degrees Celsius, and drawing up warmer water from the bottom

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24
Q

hydrophobic

A

water fearing

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25
Q

hydrophilic

A

water loving

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26
detergent
a molecule that is polar on one end and nonpolar on the other, and can thus interact with nonpolar and polar substances to mix the two.
27
acid
a proton donor
28
base
a proton acceptor
29
buffer
a substance that helps to maintain a constant pH
30
organic chemistry
the chemistry of carbon-containing molecules
31
structural isomers or constitutional isomers
molecules that have the same formula, but whose atoms are arranged differently
32
geometric isomers
molecules that have the same formula, but have atoms arranged differently about a double bond
33
Enantiomers
isomers that are mirror images of each other and are not superimposable
34
functional side groups
parts of organic molecules that have their own characteristic properties
35
the hydroxyl group
consists of an —OH
36
carbonyl group
consists of an oxygen atom double-bonded to a carbon atom (CO)
37
carboxyl group
consists of a carbon with a double-bonded oxygen atom and a hydroxyl group (COOH)
38
amine group
consists of an —NH2 group
39
carbohydrates
macromolecules that play a role in energy storage and structure
40
monosaccharides
simple one-sugar molecules that consist of carbon, hydrogen, and oxygen
41
trioses
three-carbon monosaccharides
42
pentoses
five-carbon monosaccharides
43
hexoses
six-carbon monosaccharides
44
dehydration synthesis
the process by which two monosaccharides are linked together to form a disaccharide
45
hydrolysis
the process by which a disaccharide is separated into two monosaccharides
46
monomer
a subunit of a polymer
47
glycosidic linkage
the bond between monosaccharides
48
lipids
molecules that are nonpolar and insoluble in water
49
fatty acid
a carboxylic acid consisting of a hydrocarbon chain and a terminal carboxyl group
50
ester linkage
the linkage between a fatty acid and glycerol molecule in a triglyceride
51
respiration
the process by which the energy stored in triglyceride bonds in released
52
saturated fatty acid
a fatty acid that has as many hydrogen atoms as possible on the carbon chain
53
unsaturated fatty acid
a fatty acid that has double bonds within the carbon chain, and therefore fewer hydrogen atoms
54
phospholipid
a type of lipid that has a hydrophilic, polar head, and hydrophobic, nonpolar tails
55
steroids
lipids that consist of four fused carbon rings
56
waxes
lipids that make up leaf cuticles and organ protective filters
57
nucleotides
the subunits of polymers
58
purines
two-ringed molecules that include adenine and guanine
59
pyrimidines
one-ringed molecules that include cytosine, thymine, and uracil
60
deoxyribose
the pentose sugar that makes up the nucleotides of DNA
61
ribose
the pentose sugar that makes up the nucleotides of RNA
62
what is the central dogma of biology?
DNA makes RNA, which makes proteins
63
conformation
the specific shape of a protein, as determined by its primary structure
64
R group
a group in which a carbon or hydrogen atom is attached to the rest of the molecule
65
peptide bond
a bond between amino acids, which is formed by dehyration synthesis
66
polypeptide
a chain of amino acids bonded together, with an amine group on one end and a carboxyl group on the other
67
what are the charged amino acids?
AGLAH: aspartic acid, glutamic acid, lysine, arginine, histidine
68
what are the polar amino acids?
CATTGS: cysteine, asparagine, tyrosine, threonine, glutamine, serine
69
what are the nonpolar amino acids?
PALM PIG TV: phenylalanine, alanine, methionine, proline, isoleucine, glycine, tryptophan, valine
70
primary structure
the specific sequence of amino acids in a polypeptide
71
secondary structure
the regular pattern of local hydrogen bonding within the polypeptide chain
72
tertiary structure
three-dimensional folding that results from interactions between R groups
73
hydrophobic interactions
tertiary structure interactions that occur when amino acids with hydrophobic (nonpolar) R groups fold into the center of the polypeptide because water repels them
74
Van der Waals interactions (between R groups)
in the tertiary structure of a protein, these weak interactions occur between hydrophobic (nonpolar) R groups as they fold into into the center of the polypeptide
75
ionic bonding (between R groups)
tertiary structure interactions that occur between R groups of opposite charges
76
disulfide bridges
teritary structure interactions that result in strong covalent bonds that form between two sulfhydril groups of cysteine
77
quaternary structure
the final structure of a protein that results from interactions between polypeptides
78
mutation
a change in DNA, which results in different RNA, which could result in a different sequence of amino acids, and possibly a non-functioning protein
79
the first law of thermodynamics
energy can neither be created nor destroyed
80
the second law of thermodynamics
every energy transfer results in an increase in entropy
81
entropy
the measure of randomness or disorder in a system
82
exergonic reaction
a reaction that has a negative amount of free energy, and thus gives off energy
83
catabolism
all of the metabolic processes that give off energy, and involves the breakdown of molecules
84
anabolism
all of the metabolic processes that require an input of energy. These reactions typically involve the synthesis of new molecules.
85
energy coupling
the process by which energy released from an exergonic reaction is used to feul an endergonic one
86
activation energy
the energy required to start the reaction
87
enzymes
proteins that serve as catalysts of biological reactions
88
endergonic reaction
a reaction that has a positive amount of free energy, and thus requires energy to be put into it to function
89
induced-fit model
the hypothesis for enzyme action, where the substrate induces a more complete fit of the enzyme's active site around it
90
competitive inhibitor
an inhibitor that competes with the substrate for the active site
91
noncompetitive inhibitor
an inhibitor than can bind to a part of the enzyme other than the active site permanently, ceasing that enzyme's function
92
catalytic cycle
the enzyme mechanism in which the substrate fits into the active site, the bond is broken, the products are released, and the enzyme remains intact
93
allosteric regulation
a type of enzyme regulation that uses molecules to inhibit or activate the enzyme by binding to a place other than the active site (called the allosteric site)
94
allosteric activator
an activator that binds to the enzyme and keeps it in an active state, where the active site is exposed
95
allosteric inhibitor
an inhibitor that binds to the enzyme and keeps it in an inative state, where the active site is inaccessable
96
feedback inhibition
a type of enzyme regulation that involves the inhibition of an enzyme in a metabolic pathway by an end product of that metabolic pathway
97
metabolic pathway
a process in which molecules are constructed or deconstructed. Precursor molecules are transformed in steps with an enzyme mediating each step, until the product is formed.
98
cooperativity
takes place when the binding of a substrate molecule to one subunit of an enzyme enhances the other subunits' ability to accept substrate molecules

AP Biology (14 decks)

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