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90 Terms

1
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What are the two primary functions of proteins?

structural materials and as enzymes

2
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What substances do all proteins yield upon hydrolysis?

amino acids

3
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What are proteins classified as if they yield only amino acids when hydrolyzed?

simple proteins

4
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What is the classification for proteins that yield amino acids and one or more additional products?

conjugated proteins

5
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What establishes the specific function of a protein?

the sequence of amino acids

6
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What two functional groups are present in each amino acid?

an amino group (NH2) and a carboxyl group (-COOH)

7
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What is the chemical formula given for the amino group in amino acids?

NH2

8
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What is the chemical formula given for the carboxyl group in amino acids?

-COOH

9
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What is the portion of the amino acid molecule designated as R commonly referred to?

amino acid side chain

10
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Name one type of group that the side chain (-R) of an amino acid may contain?

Alkyl groups

11
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Besides alkyl and aromatic groups, what is another group a side chain may contain?

Sulfur-containing groups

12
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Ala

Alanine

13
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Arg

Arginine

14
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Which amino acid has the abbreviation Asn?

Asparagine

15
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Aspartic acid?

Aspartic acid

16
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Cys?

Cysteine

17
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Glu

Glutamic acid

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Gln

Glutamine

19
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Which amino acid has the abbreviation Gly?

Glycine

20
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His

Histidine

21
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Ile

Isoleucine

22
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Leu

Leucine

23
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What is the abbreviation for Lysine?

Lys

24
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Met

Methionine

25
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Which amino acid is represented by the abbreviation Phe?

Phenylalanine

26
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Pro

Proline

27
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Ser

Serine

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Thr

Threonine

29
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Which amino acid has the abbreviation Trp?

Tryptophan

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Tyr

Tyrrosine

31
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Which amino acid has the abbreviation Val?

Valine

32
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What are the 10 essential amino acids?

Phenylalanine, Valine, Tryptophan, Threonine, Isoleucine, Methionine, Histidine, Arginine, Leucine, and Lysine

33
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What type of protein supplies all the essential amino acids?

complete protein

34
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What is an incomplete protein deficient in?

one or more essential amino acids

35
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Which amino acid is the only one that does not have at least one asymmetric carbon atom?

glycine

36
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What term describes amino acids because they can react either as an acid or a base?

amphoteric

37
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In what form do amino acids mainly exist even in neutral biological solutions?

zwitterions

38
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What is the name for the pH at which there is no migration toward either electrode in an electrolytic cell?

isoelectric point

39
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What is the isoelectric point of Arginine?

10.8

40
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What is the isoelectric point of Lysine?

9.7

41
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What is the isoelectric point of Alanine?

6.0

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What is the isoelectric point of Glycine?

6.0

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What is the isoelectric point of Serine?

5.7

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What is the isoelectric point of Glutamic acid?

3.2

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What is the isoelectric point of Aspartic acid?

2.9

46
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Through what structures are amino acid units joined in proteins?

amide structures

47
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What is formed when two amino acids combine and lose a molecule of water?

peptide

48
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What is the name for a molecule containing three amino acid units?

tripeptide

49
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What is the name for a molecule containing four amino acid units?

tetrapeptide

50
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What term refers to the amino acid units making up a peptide minus the elements of water?

amino acid residues

51
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In linear peptides, what is the amino-group end called?

N-terminal residue

52
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In linear peptides, what is the carboxy-group end called?

C-terminal residue

53
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How many different dipeptides can be formed from alanine and glycine?

two

54
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What two characteristics give a polypeptide its biological effectiveness and specificity?

amino acid sequence and chain length

55
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Which biological polypeptide is a pain-producing agent?

Substance P

56
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Affects tissue inflammation and blood pressure

Bradykinin

57
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Which biological polypeptide maintains water balance and blood pressure?

Angiotensin II

58
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Relieves pain, produces sense of well-being

Leu-enkephalin and Met-enkephalin

59
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Which polypeptide increases blood pressure and decreases kidney water excretion?

Vasopressin

60
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Which biological polypeptide initiates childbirth labor?

Oxytocin

61
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What are the four levels on which chemists typically describe large proteins?

Primary, Secondary, Tertiary, and Quaternary structure

62
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the number, kind, and sequence of amino acid units structure of a protein?

primary structure

63
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What determines the three-dimensional shape into which a protein folds?

the side-chain

64
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a regular three-dimensional structure held together by hydrogen bonding

Secondary structure

65
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Between which groups in the polypeptide chains does hydrogen bonding occur in secondary structures?

oxygen of the C=O and the hydrogen of the H-N groups

66
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What are two examples of protein secondary structure?

alpha-helical and beta-pleated-sheet structures

67
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distinctive and characteristic conformation, or shape

tertiary structure

68
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Name one of the three interactions mentioned that hold the tertiary structure together?

Disulfide bonding

69
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In what type of proteins is a quaternary structure found?

some complex proteins

70
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What are complex proteins with quaternary structures made of?

two or more smaller protein subunits

71
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By what type of bonds are subunits in a quaternary structure held together?

noncovalent bonds

72
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Which proteins tend to function in support roles and contain a highly developed secondary structure?

fibrous proteins

73
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What is the most abundant protein in the animal kingdom?

collagen

74
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What fibrous protein makes up hair?

Keratin

75
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What is the name of the fibrous protein found in silk?

Fibroin

76
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Where is collagen found in the body?

Tendons, ligaments, and bone matrix

77
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What protein shape is shared by myoglobin, hemoglobin, and immunoglobulin G?

globular proteins

78
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Which globular protein functions as a binding protein carrying oxygen for muscle tissue?

Myoglobin

79
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An enzyme that catalyzes protein digestion in the small intestine?

Carboxypeptidase A

80
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Which proteins bind foreign molecules as a defense against disease?

immunoglobulin G

81
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What protein has a spacefilling model where heme groups are visible in the subunits?

hemoglobin

82
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What must happen to the hemoglobin to facilitate oxygen binding in the lungs?

conformation changes

83
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What is the term for the process when a protein loses only its natural three-dimensional conformation?

denaturation

84
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Which structural levels are altered or disrupted during denaturation?

secondary, tertiary, or quaternary

85
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Which structural level is not altered during denaturation?

primary structure

86
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A protein's function depends on its natural conformation, hence a denatured protein has?

lost all biological activity

87
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What chemical reaction destroys the protein's primary sequence?

hydrolysis of the peptide bonds

88
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Three tests listed to detect and distinguish proteins and amino acids?

Xanthoproteic, Biuret. and ninhydrin

89
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Which test for proteins and amino acids starts with the letter B?

Biuret Test

90
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Which test for proteins and amino acids starts with the letter N?

Ninhydrin Test