biochem 2k26

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"term" is question, "definition" is answer

Last updated 2:01 PM on 4/25/26
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208 Terms

1
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<p>name this amino acid</p>

name this amino acid

alanine

2
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<p>name this amino acid</p>

name this amino acid

arginine

3
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<p>name this amino acid</p>

name this amino acid

asparagine

4
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<p>name this amino acid and its anionic form</p>

name this amino acid and its anionic form

aspartatic acid, aspartate

5
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<p>name this amino acid</p>

name this amino acid

cysteine

6
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<p>name this amino acid</p>

name this amino acid

glutamine

7
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<p>name this amino acid and its anionic form</p>

name this amino acid and its anionic form

glutamic acid, glutamate

8
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<p>name this amino acid</p>

name this amino acid

glycine

9
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<p>name this amino acid</p>

name this amino acid

histidine

10
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<p>name this amino acid</p>

name this amino acid

isoleucine

11
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<p>name this amino acid</p>

name this amino acid

leucine

12
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<p>name this amino acid</p>

name this amino acid

lysine

13
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<p>name this amino acid</p>

name this amino acid

methionine

14
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<p>name this amino acid</p>

name this amino acid

phenylalanine

15
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<p>name this amino acid</p>

name this amino acid

proline

16
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<p>name this amino acid</p>

name this amino acid

serine

17
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<p>name this amino acid</p>

name this amino acid

threonine

18
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<p>name this amino acid</p>

name this amino acid

tryptophan

19
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<p>name this amino acid</p>

name this amino acid

tyrosine

20
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<p>name this amino acid</p>

name this amino acid

valine

21
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<p>name this amino acid</p>

name this amino acid

selenocysteine

22
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isomers that do not have the same connectivity are:

constitutional isomers

23
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isomers that have the same connectivity are:

stereoisomers

24
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stereoisomers that cannot be separated are:

confomers

25
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stereoisomers that can be separated are:

configurational isomers

26
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two configurational isomers that behave as image and mirror image are:

chiral

27
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50:50 mixture of the two enantiomers is called:

racemate

28
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unequal mixture of two enantiomers is:

enantioenriched

29
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types of carbohydrates by the degree of polymerisation are:

monosaccharides, disaccharides, oligosaccharides, polysaccharides

30
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if a carbohydrate’s ring has 6 atoms, it is called a:

pyranose

31
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if a carbohydrate’s ring has 5 atoms, it is called a:

furanose

32
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carbohydrates can be classified based on the location of the carbonyl group as ____ and ____

aldose, ketose

33
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enantiomers have ___ chiral centers inverted

all

34
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diastereomers have ___ chiral centers inverted

some, not all

35
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diastereomers can be ___ or ___

syn, anti

36
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diastereomers of ____ systems can be adressed as cis/trans

cyclic

37
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L-arabinose has it’s lowest hydroxyl group on the ___ side in ___ projection

left, Fischer

38
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diastereomers that differ in only one asymmetric center are:

epimers

39
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saccharids have ___ and ___ anomers

alpha, beta

40
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when cholesterol is transported from liver to a different organ, it is carried in _____ system

liver protein

41
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the simplest amino acid is:

glycine

42
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only non-chiral amino acid is:

glycine

43
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only R-amino acid is:

cystein

44
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proline can greatly influence structure of proteins due to its:

cyclic structure

45
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carboxylic acid pKa is around:

5

46
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cysteine stabilizes proteins by forming:

covalent bonds

47
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peptide bonds are stiff due to similarity to:

alkenes

48
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proline causes _____ in protein structure

bends

49
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nucleoside becomes nucleotide when it is:

phosphorated

50
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____ is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst. They are usually not consumed.

cofactor

51
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the ___ amino acids encoded by our genome are all ____ amino carboxylic acids, _-amino acids (except _____) and they differ in the substitution of the ___-carbon.

20, alpha, L, glycine, alpha

52
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the only natural amino acid with _-configuration is ____ due to its ____ functional group

R, cystein, thiol

53
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hydrophobic alpha-amino acids with no additional functions are:

alanine, valine, leucine, isoleucine, methionine

54
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alpha-amino acids with polar charged groups are:

lysine, arginine, histidine, aspartic acid, glutamic acid

55
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hydrophobic alpha-amino acids with an aromatic group are:

phenylalanine, tyrosine, tryptophane

56
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alpha-amino acids with polar uncharged groups are:

serine, threonine, asparagine, glutamine

57
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<p>name this derivative of amino acid</p>

name this derivative of amino acid

cystine

58
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two of amino acid _____ can oxidize and form _____

cysteine, cystine

59
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amide bond between two amino acids is called:

peptide bond

60
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metabolic pathway where complex molecules are broken down (usually under release of energy) is:

catabolism

61
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metabolic pathway where simple molecules and energy are used to biosynthesize complex molecules is:

anabolism

62
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ATP is a double _____

anhydride

63
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during activation of carboxylic acid, following phosphate groups could be attacked:

any

64
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during first stage of catabolism fats are turned into ____, carbohydrates are turned into ____ and proteins are turned into _____

fatty acids, monosaccharides, amino acids

65
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although proteins can be digested for ATP, they are usually used for maintaining _____

muscle

66
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acetyl-CoA is an:

activated acetic acid

67
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to metabolize fatty acids they are activated with ____ molecule(s) of ____

one, ATP

68
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short- to medium-chain oligomers of amino acids are:

peptides

69
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____ is any neutral chemical compound with a positively charged cationic functional group that bears no hydrogen atom, such as a quaternary ammonium or phosphonium cation (generally: onium ions), and with a negatively charged functional group, such as a carboxylate group that may not be adjacent to the cationic site.

betaine

70
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peptide bonds have a resonance structure due to lone pair of ____ pushing into ____ orbital of ____ bond

nitrogen, pi antibonding, C-O

71
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resonance structure of a peptide bond includes a _____ between ______, which increases stiffness

double bond, nitrogen and carbon

72
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in peptide bond amide oxygen acts a strong H-bond ____ and amide nitrogen acts as strong H-bond ____

acceptor, donor

73
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peptides have structural flexibility in the bond between ____ and ____; and in bond between ____ and ____

nitrogen, alpha carbon, carbonyl carbon, alpha carbon

74
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most peptide bonds have ____ configuration, but proline is a significant contributor to ___ configuration

trans, cis

75
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the two organised local features of secondary protein structures are ____ and ____

alpha-helix, beta-pleated sheet

76
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in alpha-helix each ___ bonds to ___, ___ amino acids away

N-H, C=O, four

77
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____ does not fit into alpha-helix, and neither do ____ amino acids

proline, beta-branched

78
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beta-pleated sheets prefer ____ amino acids

small

79
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<p>name this molecule</p>

name this molecule

purine

80
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<p>name this nucleotide base</p>

name this nucleotide base

guanine

81
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<p>name this nucleotide base</p>

name this nucleotide base

adenine

82
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<p>name this nucleotide base</p>

name this nucleotide base

cytosine

83
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<p>name this nucleotide base</p>

name this nucleotide base

thymine

84
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<p>name this nucleotide base</p>

name this nucleotide base

uracil

85
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<p>name this molecule</p>

name this molecule

pyrimidine

86
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nucleosides employ either ___ or ___ as sugars

ribose, 2-deoxyribose

87
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<p>name this saccharide</p>

name this saccharide

beta-D-ribofuranose

88
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<p>name this saccharide</p>

name this saccharide

alpha-D-ribopyranose

89
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<p>name this saccharide</p>

name this saccharide

2-desoxyribose

90
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in nucleosides, nucleobases are linked to the furanose via its ____ center

anomeric

91
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the carbon where a sugar’s ring closure occurs is the ___ carbon

anomeric

92
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<p>name this nucleoside</p>

name this nucleoside

adenosine

93
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in a nucleoside, the anomeric carbon is linked through a glycosidic bond to the N_ of a purine or the N_ of a pyrimidine

9, 1

94
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<p>name this nucleoside</p>

name this nucleoside

guanosine

95
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<p>name this nucleoside</p>

name this nucleoside

cytidine

96
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<p>name this nucleoside</p>

name this nucleoside

uridine

97
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<p>name this nucleoside</p>

name this nucleoside

2’-deoxyadenosine

98
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<p>name this nucleoside</p>

name this nucleoside

2’-deoxyguanosine

99
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<p>name this nucleoside</p>

name this nucleoside

2’-deoxycytidine

100
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<p>name this nucleoside</p>

name this nucleoside

thymidine (deoxythymidine)