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

Chapter 2: Inorganic and Organic Chemistry Flashcards

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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
Q

detergent

A

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.

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27
Q

acid

A

a proton donor

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28
Q

base

A

a proton acceptor

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29
Q

buffer

A

a substance that helps to maintain a constant pH

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30
Q

organic chemistry

A

the chemistry of carbon-containing molecules

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31
Q

structural isomers or constitutional isomers

A

molecules that have the same formula, but whose atoms are arranged differently

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32
Q

geometric isomers

A

molecules that have the same formula, but have atoms arranged differently about a double bond

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33
Q

Enantiomers

A

isomers that are mirror images of each other and are not superimposable

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34
Q

functional side groups

A

parts of organic molecules that have their own characteristic properties

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35
Q

the hydroxyl group

A

consists of an —OH

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36
Q

carbonyl group

A

consists of an oxygen atom double-bonded to a carbon atom (CO)

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37
Q

carboxyl group

A

consists of a carbon with a double-bonded oxygen atom and a hydroxyl group (COOH)

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38
Q

amine group

A

consists of an —NH2 group

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39
Q

carbohydrates

A

macromolecules that play a role in energy storage and structure

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40
Q

monosaccharides

A

simple one-sugar molecules that consist of carbon, hydrogen, and oxygen

41
Q

trioses

A

three-carbon monosaccharides

42
Q

pentoses

A

five-carbon monosaccharides

43
Q

hexoses

A

six-carbon monosaccharides

44
Q

dehydration synthesis

A

the process by which two monosaccharides are linked together to form a disaccharide

45
Q

hydrolysis

A

the process by which a disaccharide is separated into two monosaccharides

46
Q

monomer

A

a subunit of a polymer

47
Q

glycosidic linkage

A

the bond between monosaccharides

48
Q

lipids

A

molecules that are nonpolar and insoluble in water

49
Q

fatty acid

A

a carboxylic acid consisting of a hydrocarbon chain and a terminal carboxyl group

50
Q

ester linkage

A

the linkage between a fatty acid and glycerol molecule in a triglyceride

51
Q

respiration

A

the process by which the energy stored in triglyceride bonds in released

52
Q

saturated fatty acid

A

a fatty acid that has as many hydrogen atoms as possible on the carbon chain

53
Q

unsaturated fatty acid

A

a fatty acid that has double bonds within the carbon chain, and therefore fewer hydrogen atoms

54
Q

phospholipid

A

a type of lipid that has a hydrophilic, polar head, and hydrophobic, nonpolar tails

55
Q

steroids

A

lipids that consist of four fused carbon rings

56
Q

waxes

A

lipids that make up leaf cuticles and organ protective filters

57
Q

nucleotides

A

the subunits of polymers

58
Q

purines

A

two-ringed molecules that include adenine and guanine

59
Q

pyrimidines

A

one-ringed molecules that include cytosine, thymine, and uracil

60
Q

deoxyribose

A

the pentose sugar that makes up the nucleotides of DNA

61
Q

ribose

A

the pentose sugar that makes up the nucleotides of RNA

62
Q

what is the central dogma of biology?

A

DNA makes RNA, which makes proteins

63
Q

conformation

A

the specific shape of a protein, as determined by its primary structure

64
Q

R group

A

a group in which a carbon or hydrogen atom is attached to the rest of the molecule

65
Q

peptide bond

A

a bond between amino acids, which is formed by dehyration synthesis

66
Q

polypeptide

A

a chain of amino acids bonded together, with an amine group on one end and a carboxyl group on the other

67
Q

what are the charged amino acids?

A

AGLAH: aspartic acid, glutamic acid, lysine, arginine, histidine

68
Q

what are the polar amino acids?

A

CATTGS: cysteine, asparagine, tyrosine, threonine, glutamine, serine

69
Q

what are the nonpolar amino acids?

A

PALM PIG TV: phenylalanine, alanine, methionine, proline, isoleucine, glycine, tryptophan, valine

70
Q

primary structure

A

the specific sequence of amino acids in a polypeptide

71
Q

secondary structure

A

the regular pattern of local hydrogen bonding within the polypeptide chain

72
Q

tertiary structure

A

three-dimensional folding that results from interactions between R groups

73
Q

hydrophobic interactions

A

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
Q

Van der Waals interactions (between R groups)

A

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
Q

ionic bonding (between R groups)

A

tertiary structure interactions that occur between R groups of opposite charges

76
Q

disulfide bridges

A

teritary structure interactions that result in strong covalent bonds that form between two sulfhydril groups of cysteine

77
Q

quaternary structure

A

the final structure of a protein that results from interactions between polypeptides

78
Q

mutation

A

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
Q

the first law of thermodynamics

A

energy can neither be created nor destroyed

80
Q

the second law of thermodynamics

A

every energy transfer results in an increase in entropy

81
Q

entropy

A

the measure of randomness or disorder in a system

82
Q

exergonic reaction

A

a reaction that has a negative amount of free energy, and thus gives off energy

83
Q

catabolism

A

all of the metabolic processes that give off energy, and involves the breakdown of molecules

84
Q

anabolism

A

all of the metabolic processes that require an input of energy. These reactions typically involve the synthesis of new molecules.

85
Q

energy coupling

A

the process by which energy released from an exergonic reaction is used to feul an endergonic one

86
Q

activation energy

A

the energy required to start the reaction

87
Q

enzymes

A

proteins that serve as catalysts of biological reactions

88
Q

endergonic reaction

A

a reaction that has a positive amount of free energy, and thus requires energy to be put into it to function

89
Q

induced-fit model

A

the hypothesis for enzyme action, where the substrate induces a more complete fit of the enzyme’s active site around it

90
Q

competitive inhibitor

A

an inhibitor that competes with the substrate for the active site

91
Q

noncompetitive inhibitor

A

an inhibitor than can bind to a part of the enzyme other than the active site permanently, ceasing that enzyme’s function

92
Q

catalytic cycle

A

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
Q

allosteric regulation

A

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
Q

allosteric activator

A

an activator that binds to the enzyme and keeps it in an active state, where the active site is exposed

95
Q

allosteric inhibitor

A

an inhibitor that binds to the enzyme and keeps it in an inative state, where the active site is inaccessable

96
Q

feedback inhibition

A

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
Q

metabolic pathway

A

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
Q

cooperativity

A

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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