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BCHEM 2ND SHIFT > LAB: EXP 2 (Isolation of Proteins) > Flashcards

LAB: EXP 2 (Isolation of Proteins) Flashcards

1
Q

Proteins are made up of smaller units called _____

A

amino acids

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2
Q

They are essential for the structure, function, and regulation of the body tissues and organs

A

Proteins

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3
Q

Amino acids that have an amino group bonded directly to the alpha-carbon are referred to as _____

A

alpha amino acids

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4
Q

the polar group is a hydroxyl (-OH) bonded to aliphatic hydrocarbon groups

A

serine and threonine

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5
Q

the hydroxyl group (phenol) is bonded to an aromatic hydrocarbon group

A

tyrosine

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6
Q

the polar side chain contains a thiol group (-SH)

A

cysteine

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7
Q

contain amide groups in their side chains

A

Glutamine and asparagine

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8
Q

Acidic amino acids

A

Glutamic acid, aspartic acid

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9
Q

Basic amino acids

A

Histidine, lysine, and arginine

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10
Q

Classification of amino acids according to polarity

A
  • Uncharged non-polar
  • Uncharged polar
  • Charge polar
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11
Q

Classification of amino acids according to nutritional availability

A
  • Non-essential
  • Essential
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12
Q

Amino acids are linked together by ‘amide groups’ called _____.

A

peptide bonds

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13
Q

During protein synthesis, the carboxyl group of amino acid at the end of the growing polypeptide chain reacts with the amino group of an incoming amino acid, releasing a molecule of _____

A

water

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14
Q

Amino acid links to another to form a peptide through _____ and _____

A

peptide bond, condensation

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15
Q

Identify the structure: Sequence of amino acid residues that serves as the backbone of a peptide chain or protein

A

Primary

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16
Q

Function of the protein depends on the _____ structure

A

primary

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17
Q

Identify the structure: Regular, repeating folding patterns

A

secondary

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18
Q

Identify the structure: the “local” ordered structure brought about via H-bonding mainly

A

secondary

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19
Q

Identify the structure: α-helix & β-pleated sheets

A

secondary

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20
Q

Identify whether α-helix or β-pleated sheets: Rod-like structure

A

α-helix

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21
Q

Identify whether α-helix or β-pleated sheets: N-H to C=O

A

α-helix

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22
Q

Identify whether α-helix or β-pleated sheets: H-bonds in 4th succeeding amino acids

A

α-helix

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23
Q

Identify whether α-helix or β-pleated sheets: H-bonds parallel to axis

A

α-helix

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24
Q

Identify whether α-helix or β-pleated sheets: typically amphiphilic

A

α-helix

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25
Q

Identify whether α-helix or β-pleated sheets: polypeptide chains are arranged side by side

A

β-pleated sheets

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26
Q

Identify whether α-helix or β-pleated sheets: H-bonds form between chains

A

β-pleated sheets

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27
Q

Identify whether α-helix or β-pleated sheets: parallel or antiparallel

A

β-pleated sheets

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28
Q

Identify whether α-helix or β-pleated sheets: more stable

A

β-pleated sheets

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29
Q

Identify the structure: The way the segments of the protein fold in 3 dimensions

A

tertiary

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30
Q

Identify the structure: overall folding of domains

A

tertiary

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31
Q

Identify the structure: specific overall shape of a protein

A

tertiary

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32
Q

Identify the structure: cross links between R-groups of amino acids

A

tertiary

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33
Q

Cross links in tertiary structures happen in:

A

o Disulfide
o Ionic
o Hydrophobic

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34
Q

Identify the structure: Interaction between different polypeptide chains to produce an oligomeric structure

A

quaternary

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35
Q

Identify the structure: Aggregates of two or more protein chain connected by weak non-covalent interactions

A

quaternary

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36
Q

Identify the structure: Proteins with two or more chains

A

quaternary

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37
Q

Yield only amino acids upon hydrolysis

A

Simple proteins

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38
Q

Simple proteins + non-protein substances

A

Conjugated proteins

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39
Q

Catalytic protein example

A

Enzymes

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40
Q

Transport protein examples

A

Hemoglobin, transferrin, albumin

41
Q

Storage protein examples

A

Ovalbumin, casein, gliadin

42
Q

Contraction protein examples

A

Actin, myosin

43
Q

Gene regulation protein examples

A

Histones, non-histone nuclear

44
Q

Regulatory protein examples

A

Hormone, repressor proteins

45
Q

Immune protein examples

A

Antibodies, fibrin, complement

46
Q

Structural protein examples

A

Collagen, elastin, keratin

47
Q

Neurotransmission protein examples

A

Receptor proteins

48
Q

polypeptide chain/s folded into spherical or globular shape

A

globular protein

49
Q

soluble in aq. system

A

globular protein

50
Q

polypeptide chains arranged in long strands or sheets

A

fibrous protein

51
Q

water insoluble

A

fibrous protein

52
Q

Soluble in water and dilute aqueous solutions

A

Albumins (Plasma)

53
Q

Soluble in dilute salt solutions but are insoluble or sparingly soluble in water

A

Globulins (Serum)

54
Q

Soluble in dilute solutions of acids and bases; insoluble in neutral solvents

A

Glutelins (Flour)

55
Q
  • Soluble 50-90% alcohol
  • Insoluble in water, neutral solvents, or absolute alcohol
A

Prolamins (Store protein in plants)

56
Q

Albumin-like that is insoluble in most ordinary solvents

A

Albuminoids/Scleroproteins

57
Q

A loss of three-dimensional structure sufficient to cause of loss of function

A

Protein Denaturation

58
Q

Denaturating agents

A
  • Strong acids and bases
  • Organic solvents
  • Detergents
  • Reducing agents
  • Salts (salting in and salting out)
  • Heavy metals
  • Temperature
59
Q

Type of protein hydrolysis: uses a strong acid or base + high temperature

A

Complete hydrolysis

60
Q

Type of hydrolysis: Most commonly used reagent is 6N HCl

A

Acid hydrolysis

61
Q

In acid hydrolysis: ___ and ___ are partially destroyed

A

cys and tyr

62
Q

In acid hydrolysis, ___ is completely destroyed

63
Q

In acid hydrolysis, ___ and ___ are incompletely liberated

A

val and ile

64
Q

In acid hydrolysis, ___ and ___ are racemized and destroyed

A

ser and thr

65
Q

Type of hydrolysis: uses NaOH or KOH

A

basic hydrolysis

66
Q

Advantage of basic hydrolysis

A

trp not destroyed

67
Q

Disadvantage of basic hydrolysis

A

arg, asn, gln, ser are destroyed

68
Q

Type of hydrolysis: uses enzyme called protease

A

Incomplete/partial hydrolysis

69
Q

_____ (eg. acid, base, enzyme) are needed to facilitate the hydrolysis of peptide bonds

70
Q

type of hydrolysis: presence of proteolytic enzymes results to partial or selective hydrolysis of polypeptide to yield a mixture of peptide fragments.

A

Enzymatic hydrolysis

71
Q

enzymes that hydrolyze peptide bonds at specific sites

A

proteases/peptidases

72
Q

Advantage of incomplete/partial hydrolysis

A

Amino acids are not affected

73
Q

Type of hydrolysis: requires certain temperature & pH conditions for optimum activity of enzymes

A

Incomplete/Partial hydrolysis

74
Q

Type of exopeptidase: cuts C-terminal residues except R,K and P

A

Carboxypeptidase A

75
Q

Type of exopeptidase: cuts C-terminal residues except R,K

A

Carboxypeptidase B

76
Q

Type of exopeptidase: cuts most N-terminal except when P is the next residue

A

Aminopeptidase

77
Q

Type of endopeptidase: cuts C side R & K

78
Q

Type of endopeptidase: cuts C side of F, Y, W

A

Chymotrypsin

79
Q

Type of endopeptidase: cuts C side of hydrophobic groups/aromatic R-groups

80
Q

Used in precipitation separation method and their solubility

A
  • ammonium sulfate (sol)
  • polyethylene glycol (sol)
81
Q

Properties of proteins being considered during separation

A

o Charge
o Molecular size, shape
o Solubility
o Affinity to a ligand
o pI/IpH

82
Q

A procedure in which the pH of the protein mixture is adjusted to the pI of the protein to be isolated to selectively minimize its solubility.

A

Change in pH

82
Q

Casein: source and isolation method

A
  • Source: Skimmed milk
  • Isolation method: Isoelectric precipitation
83
Q

Casein: type of protein

A

Phosphoprotein

84
Q

Isoelectric point of casein

85
Q

Mechanism of casein separation

A

PO4—3 interacts (ionic) with Ca+2 leading to polymerization of casein

86
Q

Albumin: source and isolation method

A
  • Source: Skimmed milk
  • Isolation method: Denaturation and Coagulation by heat
87
Q

Albumin: type of protein

A

Globular protein (sol in water and diluted salt solutions)

88
Q

Second major protein in bovine milk and can serve as a regulator protein in lactose biosynthesis

89
Q

Albumin is a _____ that can bind to several metal ions like calcium and zinc

A

metalloprotein

90
Q

Myoglobin: source and isolation method

A
  • Source: Beef muscle
  • Isolation method: Salt-induced precipitation
91
Q

Color of isolated myoglobin precipitate

92
Q

Gluten: source and isolation method

A
  • Source: Wheat flour
  • Isolation method: Solubility difference
93
Q

Gives bread its structure, texture, and elasticity

94
Q

Gluten is a composite of _____ and ____, which exist, conjoined with starch

A

Prolamin and glutelin

95
Q

T/F: the isolated gluten should be positive of the iodin test

A

F. Should be negative.

96
Q

Role of gluten in bread making

A

traps the CO2 and gives off chewiness

97
Q

Solution used to test the complete removal of starch

98
Q

Appearance of isolated gluten

A

Yellowish-white solid, tough, elastic, sticky

BCHEM 2ND SHIFT (7 decks)

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