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AP Biology > Chapter 4 & 5 - Carbon and the Molecular Diversity of Life & The Structure and Function of Large Biological Molecules > Flashcards

Chapter 4 & 5 - Carbon and the Molecular Diversity of Life & The Structure and Function of Large Biological Molecules Flashcards

1
Q

study of carbon containing compounds

A

organic chemistry

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2
Q

the number of covalent bonds an atom can form

A

valence

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3
Q

organic molecules consisting of only carbon and hydrogen

A

hydrocarbons

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4
Q

compounds that have the same numbers of atoms of the same elements but different structures and properties

A

isomers

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5
Q

differ in the covalent arrangements of their atoms

A

structural isomers

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6
Q

carbons have covalent bonds to the same atoms, but these atoms differ in their spatial arrangements due to the inflexibility of double bonds

A

cis-trans isomers (geometric isomers)

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7
Q

isomers that are mirror images of each other and differ in shape due to the presence of an asymmetric carbon

A

enantiomers

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8
Q

carbon that is attached to four different atoms or groups of atoms

A

asymmetric carbon

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9
Q

chemical groups that are directly involved in chemical reactions

A

functional groups

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10
Q

–OH

A

hydroxyl group

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11
Q

C=O

A

carbonyl group

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12
Q

-COOH

A

carboxyl group

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13
Q

–NH2

A

amino group

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14
Q

–SH

A

sulfhydryl group

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15
Q

–OPO3 2-

A

Phosphate group

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16
Q

–CH3

A

methyl group

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17
Q

large carbohydrates, proteins, and nucleic acids

A

macromolecules

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18
Q

long molecule consisting of many similar or identical building blocks linked by covalent bonds

A

polymer

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19
Q

repeating units that serve as the building blocks of a polymer - are smaller molecules

A

monomers

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20
Q

specialized macromolecules that speed up chemical reactions

A

enzymes

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21
Q

a reaction in which two molecules are covalently bonded to each other with the loss of a water molecule

A

dehydration synthesis

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22
Q

process that is the reverse of dehydration synthesis

A

hydrolysis

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23
Q

carbohydrate that is called a single sugar – made of CH2O

A

monosaccharides

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24
Q

consists of two monosaccharides joined by a glycosidic linkage

A

disaccharide

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25
Q

a covalent bond formed between two monosaccharides by a dehydration reaction

A

glycosidic linkage

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26
Q

macromolecules, polymers with a few hundred to thousand monosaccharides joined by glycosidic linkages

A

polysaccharides

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27
Q

a polymer of glucose monomers

A

starch

28
Q

a polymer of glucose that is like amylopectin but more extensively branched

A

glycogen

29
Q

polysaccharide that is a major component of the touch walls that enclose plant cells

A

cellulose

30
Q

the carbohydrate used by arthropods to build their exoskeletons

A

chitin

31
Q

compounds are grouped together because they are hydrophobic

A

lipids

32
Q

long carbon skeleton, usually 16 to 18 carbon atoms in length

A

fatty acid

33
Q

`

A
34
Q

no double bond in a fatty acid

A

saturated fatty acid

35
Q

fatty acid with one or more double bonds

A

unsaturated fatty acids

36
Q

similar to a fat molecule but has only two fatty acids attached to glycerol

A

phospholipid

37
Q

lipids characterized by a carbon skeleton consisting of 4 fused rings

A

steroids

38
Q

type of steroid that is crucial in all animals

A

cholesterol

39
Q

chemical agents that selectively speed up chemical reactions without being consumed in the reaction

A

catalysts

40
Q

polymer of amino acids

A

polypeptide

41
Q

biologically functional molecule made up of one or more polypeptides each folded and coiled into a specific 3D structure

A

protein

42
Q

organic molecule with both an amino group and a carboxyl group

A

amino acid

43
Q

covalent bond resulting from two amino acids becoming joined by a dehydration reaction

A

peptide bond

44
Q

sequence of amino acids (linear chain of amino acid)

A

primary structure

45
Q

segments of polypeptide chains repeatedly coiled or folded in patterns
(regions stabilized by hydrogen bonds between atoms of the polypeptide backbone)

A

secondary structure

46
Q

delicate coil held together by hydrogen bonding between every 4th amino acid

A

alpha helix

47
Q

two or more segments of polypeptide chain lying side by side are connected by hydrogen bonds between parts of the two parallel segments

A

beta pleated sheets

48
Q

overall shape of a polypeptide resulting from interactions between the side chains of various amino acids
(3D shape stabilized by interactions between side chains)

A

tertiary structure

49
Q

as polypeptide folds into its functional shape, amino acids with hydrophobic side chains usually end up in clusters at the core of the protein

A

hydrophobic interaction

50
Q

form where two cysteine monomers are brought together by the folding of the protein

A

disulfide bridges

51
Q

overall protein structure that results form the combination of polypeptide subunits
(association of two or more polypeptides) ONLY SOME PROTEINS

A

quaternary structure

52
Q

when protein unravels and loses its native shape

A

denaturation

53
Q

unit of inheritance

A

gene

54
Q

polymers made of monomers called nucleotides

A

nucleic acids

55
Q

nucleic acids are macromolecules that exist as polymers

A

polynucleotides

56
Q

has one 6-membered ring of carbon and nitrogen atoms

A

pyrimidine

57
Q

List the pyrimidines

A

cytosine, thymine, uracil

58
Q

larger, with 6-membered ring fused to a 5-membered ring

A

purines

59
Q

list the purines

A

adenine and guanine

60
Q

sugar in DNA

A

deoxyribose

61
Q

sugar in RNA

A

ribose

62
Q

the 2 sugar phosphate backbones in DNA run __________ of each other.

A

antiparallel

63
Q

the use of computer software and other computational tools that can handle and analyze these large data sets

A

bioinformatics

64
Q

analyzing large sets of genes or even comparing whole genomes of different species

A

genomics

65
Q

analysis of large sets of proteins and their sequences

A

proteomics

AP Biology (2 decks)

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