PROTEINS TESTS

PROTEINS TESTS
82問 • 1年前
  • saoirse
  • 通報

    問題一覧

  • 1

    It is the general test for the identification of proteins.

    biuret test

  • 2

    This is the positive result for biuret test.

    purple solution

  • 3

    Biuret test is positive for all compounds containing ________.

    peptide bonds

  • 4

    BIURET, POSITIVE OR NEGATIVE: gelatin

    positive

  • 5

    BIURET, POSITIVE OR NEGATIVE: egg albumin

    positive

  • 6

    BIURET, POSITIVE OR NEGATIVE: casein

    positive

  • 7

    BIURET, POSITIVE OR NEGATIVE: glycine

    negative

  • 8

    BIURET, POSITIVE OR NEGATIVE: protein hydrolyzate

    negative

  • 9

    Glycine tested negative for Biuret Test because instead of a peptide bond, it contains a single __________.

    amino acid

  • 10

    This is the test for the presence of α-amino acid in proteins.

    ninhydrin

  • 11

    This is the positive result for a Ninhydrin Test.

    blue

  • 12

    NINHYDRIN, POSITIVE OR NEGATIVE: egg albumin

    positive

  • 13

    BIURET, POSITIVE OR NEGATIVE: gelatin

    positive

  • 14

    BIURET, POSITIVE OR NEGATIVE: protein hydrolyzate

    positive

  • 15

    BIURET, POSITIVE OR NEGATIVE: alanine

    positive

  • 16

    BIURET, POSITIVE OR NEGATIVE: proline

    negative

  • 17

    Prolein tested negative for Ninhydrin Test because instsad of an alpha-amino acid, prolein is an __________.

    imino acid

  • 18

    This is the test for the presence of aromatic amino acids.

    Xanthoproteic test

  • 19

    This is the positive result for Xanthoproteic test.

    yellow to red-orange

  • 20

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: egg albumin

    positive

  • 21

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: tyrosine

    positive

  • 22

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: alanine

    negative

  • 23

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: casein

    positive

  • 24

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: phenylalanine

    positive

  • 25

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: protein hydrolyzate

    positive

  • 26

    Gelatin turned out to be this color because it only contains traces of phenylalanine and tyrosine.

    light orange

  • 27

    This is the test for phenolic compounds.

    millon’s test

  • 28

    Millon’s Test tests for this amino acid because this amino acid is the only one to contain a phenol group.

    tyrosine

  • 29

    Whether a precipitate or a complete change in color of solution, this is the positive result for Millon’s Test.

    red

  • 30

    MILLON, POSITIVE OR NEGATIVE: protein hydrolyzate

    positive

  • 31

    MILLON, POSITIVE OR NEGATIVE: alanine

    negative

  • 32

    MILLON, POSITIVE OR NEGATIVE: tyrosine

    positive

  • 33

    MILLON, POSITIVE OR NEGATIVE: phenol

    positive

  • 34

    MILLON, POSITIVE OR NEGATIVE: albumin

    positive

  • 35

    Gelatin only contains traces of tyrosine, so its resulting color is only _______.

    light pinkish-red

  • 36

    This is the test for tryptophan.

    hopkins cole

  • 37

    This is the only amino acid containing an indole group, which is being tested in the Hopkins Cole Test.

    tryptophan

  • 38

    This is the positive result for Hopkins Cole Test.

    violet ring

  • 39

    HOPKINS, POSITIVE OR NEGATIVE: albumin

    positive

  • 40

    HOPKINS, POSITIVE OR NEGATIVE: casein

    positive

  • 41

    HOPKINS, POSITIVE OR NEGATIVE: gelatin

    negative

  • 42

    HOPKINS, POSITIVE OR NEGATIVE: tryptophan

    positive

  • 43

    HOPKINS, POSITIVE OR NEGATIVE: protein hydrolyzate

    positive

  • 44

    This is the test for the presence of cysteine or cystine.

    SH

  • 45

    This is the positive result for SH Test.

    black precipitate

  • 46

    SH, POSITIVE OR NEGATIVE: albumin

    positive

  • 47

    SH, POSITIVE OR NEGATIVE: tyrosine

    negative

  • 48

    SH, POSITIVE OR NEGATIVE: casein

    negative

  • 49

    SH, POSITIVE OR NEGATIVE: gelatin

    positive

  • 50

    SH, POSITIVE OR NEGATIVE: methionine

    negative

  • 51

    This type of denaturation occurs in gently heating a protein.

    reversible

  • 52

    This type of denaturation occurs in vigorously heating a protein.

    irreversible

  • 53

    REACTION WITH HEAT, POSITIVE OR NEGATIVE: albumin

    positive

  • 54

    REACTION WITH HEAT, POSITIVE OR NEGATIVE: gelatin

    negative

  • 55

    REACTION WITH HEAT, POSITIVE OR NEGATIVE: casein

    negative

  • 56

    What formed upon heating albumin?

    white coagulate

  • 57

    Gelatin and casein did not form a coagulate upon heating as they are categorized as

    non-heat coagulable protein

  • 58

    Mercuric chloride, silver nitrate, and lead precipitate proteins are examples of

    heavy metal salts

  • 59

    Heavy metal salts denature proteins irreversibly by disrupting the ____________ and ______________.

    salt bridges, disulfide bonds

  • 60

    Albumin with silver nitrate resulted in

    more coagulation

  • 61

    Albumin with mercuric chloride resulted in

    lesser coagulation

  • 62

    Alkaloidal reagents combine with positively charged amino groups in proteins to disrupt this type of bond.

    ionic

  • 63

    These reagents form insoluble compounds with protein.

    alkaloidal reagents

  • 64

    Albumin and picric acid resulted in this color of coagulate.

    yellow

  • 65

    Albumin and tannic acid resulted in this color of coagulate.

    light brown

  • 66

    Albumin and TCA resulted in this color of coagulate.

    white

  • 67

    A change in this power can disrupt hydrogen bonds and salt bridges, causing irreversible denaturation.

    pH

  • 68

    Concentrated HCl, H2SO4, and HNO3 are examples of _______.

    strong acids

  • 69

    Albumin and HNO3 resulted in this color of coagulate.

    yellow

  • 70

    Albumin and HCl resulted in this color of coagulate.

    white

  • 71

    The excess HNO3 in the Albumin and HNO3 reaction produced a solution of this color.

    yellow

  • 72

    The excess HCl in the Albumin and HCl reaction produced a solution of this color.

    colorless

  • 73

    They alter the native structure of proteins by disrupting hydrophobic interactions between the nonpolar side chains of amino acids.

    organic solvents

  • 74

    Alcohol coagulates all types of protein except?

    prolamine

  • 75

    This irreversibly denatures by forming hydrogen bonds that compete with the naturally occurring hydrogen bonds in the protein.

    alcohol

  • 76

    Albumin in a 95% ethanol produces this amount of white coagulate.

    excessive

  • 77

    Albumin in a 70% ethanol produces this amount of white coagulate.

    moderate

  • 78

    Albumin in a 40% ethanol produces this amount of white coagulate.

    small

  • 79

    95% ethanol only denatures ________.

    surface proteins

  • 80

    70% ethanol penetrates bacteria and kills them by doing this to their proteins.

    coagulate

  • 81

    Only small amounts of coagulate are produced by 40% ethanol because they are _______.

    too diluted

  • 82

    It denatures protein irreversibly by breaking disulfide bonds and reducing them to SH.

    reducing agents

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    問題一覧

  • 1

    It is the general test for the identification of proteins.

    biuret test

  • 2

    This is the positive result for biuret test.

    purple solution

  • 3

    Biuret test is positive for all compounds containing ________.

    peptide bonds

  • 4

    BIURET, POSITIVE OR NEGATIVE: gelatin

    positive

  • 5

    BIURET, POSITIVE OR NEGATIVE: egg albumin

    positive

  • 6

    BIURET, POSITIVE OR NEGATIVE: casein

    positive

  • 7

    BIURET, POSITIVE OR NEGATIVE: glycine

    negative

  • 8

    BIURET, POSITIVE OR NEGATIVE: protein hydrolyzate

    negative

  • 9

    Glycine tested negative for Biuret Test because instead of a peptide bond, it contains a single __________.

    amino acid

  • 10

    This is the test for the presence of α-amino acid in proteins.

    ninhydrin

  • 11

    This is the positive result for a Ninhydrin Test.

    blue

  • 12

    NINHYDRIN, POSITIVE OR NEGATIVE: egg albumin

    positive

  • 13

    BIURET, POSITIVE OR NEGATIVE: gelatin

    positive

  • 14

    BIURET, POSITIVE OR NEGATIVE: protein hydrolyzate

    positive

  • 15

    BIURET, POSITIVE OR NEGATIVE: alanine

    positive

  • 16

    BIURET, POSITIVE OR NEGATIVE: proline

    negative

  • 17

    Prolein tested negative for Ninhydrin Test because instsad of an alpha-amino acid, prolein is an __________.

    imino acid

  • 18

    This is the test for the presence of aromatic amino acids.

    Xanthoproteic test

  • 19

    This is the positive result for Xanthoproteic test.

    yellow to red-orange

  • 20

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: egg albumin

    positive

  • 21

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: tyrosine

    positive

  • 22

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: alanine

    negative

  • 23

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: casein

    positive

  • 24

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: phenylalanine

    positive

  • 25

    XANTHOPROTEIC, POSITIVE OR NEGATIVE: protein hydrolyzate

    positive

  • 26

    Gelatin turned out to be this color because it only contains traces of phenylalanine and tyrosine.

    light orange

  • 27

    This is the test for phenolic compounds.

    millon’s test

  • 28

    Millon’s Test tests for this amino acid because this amino acid is the only one to contain a phenol group.

    tyrosine

  • 29

    Whether a precipitate or a complete change in color of solution, this is the positive result for Millon’s Test.

    red

  • 30

    MILLON, POSITIVE OR NEGATIVE: protein hydrolyzate

    positive

  • 31

    MILLON, POSITIVE OR NEGATIVE: alanine

    negative

  • 32

    MILLON, POSITIVE OR NEGATIVE: tyrosine

    positive

  • 33

    MILLON, POSITIVE OR NEGATIVE: phenol

    positive

  • 34

    MILLON, POSITIVE OR NEGATIVE: albumin

    positive

  • 35

    Gelatin only contains traces of tyrosine, so its resulting color is only _______.

    light pinkish-red

  • 36

    This is the test for tryptophan.

    hopkins cole

  • 37

    This is the only amino acid containing an indole group, which is being tested in the Hopkins Cole Test.

    tryptophan

  • 38

    This is the positive result for Hopkins Cole Test.

    violet ring

  • 39

    HOPKINS, POSITIVE OR NEGATIVE: albumin

    positive

  • 40

    HOPKINS, POSITIVE OR NEGATIVE: casein

    positive

  • 41

    HOPKINS, POSITIVE OR NEGATIVE: gelatin

    negative

  • 42

    HOPKINS, POSITIVE OR NEGATIVE: tryptophan

    positive

  • 43

    HOPKINS, POSITIVE OR NEGATIVE: protein hydrolyzate

    positive

  • 44

    This is the test for the presence of cysteine or cystine.

    SH

  • 45

    This is the positive result for SH Test.

    black precipitate

  • 46

    SH, POSITIVE OR NEGATIVE: albumin

    positive

  • 47

    SH, POSITIVE OR NEGATIVE: tyrosine

    negative

  • 48

    SH, POSITIVE OR NEGATIVE: casein

    negative

  • 49

    SH, POSITIVE OR NEGATIVE: gelatin

    positive

  • 50

    SH, POSITIVE OR NEGATIVE: methionine

    negative

  • 51

    This type of denaturation occurs in gently heating a protein.

    reversible

  • 52

    This type of denaturation occurs in vigorously heating a protein.

    irreversible

  • 53

    REACTION WITH HEAT, POSITIVE OR NEGATIVE: albumin

    positive

  • 54

    REACTION WITH HEAT, POSITIVE OR NEGATIVE: gelatin

    negative

  • 55

    REACTION WITH HEAT, POSITIVE OR NEGATIVE: casein

    negative

  • 56

    What formed upon heating albumin?

    white coagulate

  • 57

    Gelatin and casein did not form a coagulate upon heating as they are categorized as

    non-heat coagulable protein

  • 58

    Mercuric chloride, silver nitrate, and lead precipitate proteins are examples of

    heavy metal salts

  • 59

    Heavy metal salts denature proteins irreversibly by disrupting the ____________ and ______________.

    salt bridges, disulfide bonds

  • 60

    Albumin with silver nitrate resulted in

    more coagulation

  • 61

    Albumin with mercuric chloride resulted in

    lesser coagulation

  • 62

    Alkaloidal reagents combine with positively charged amino groups in proteins to disrupt this type of bond.

    ionic

  • 63

    These reagents form insoluble compounds with protein.

    alkaloidal reagents

  • 64

    Albumin and picric acid resulted in this color of coagulate.

    yellow

  • 65

    Albumin and tannic acid resulted in this color of coagulate.

    light brown

  • 66

    Albumin and TCA resulted in this color of coagulate.

    white

  • 67

    A change in this power can disrupt hydrogen bonds and salt bridges, causing irreversible denaturation.

    pH

  • 68

    Concentrated HCl, H2SO4, and HNO3 are examples of _______.

    strong acids

  • 69

    Albumin and HNO3 resulted in this color of coagulate.

    yellow

  • 70

    Albumin and HCl resulted in this color of coagulate.

    white

  • 71

    The excess HNO3 in the Albumin and HNO3 reaction produced a solution of this color.

    yellow

  • 72

    The excess HCl in the Albumin and HCl reaction produced a solution of this color.

    colorless

  • 73

    They alter the native structure of proteins by disrupting hydrophobic interactions between the nonpolar side chains of amino acids.

    organic solvents

  • 74

    Alcohol coagulates all types of protein except?

    prolamine

  • 75

    This irreversibly denatures by forming hydrogen bonds that compete with the naturally occurring hydrogen bonds in the protein.

    alcohol

  • 76

    Albumin in a 95% ethanol produces this amount of white coagulate.

    excessive

  • 77

    Albumin in a 70% ethanol produces this amount of white coagulate.

    moderate

  • 78

    Albumin in a 40% ethanol produces this amount of white coagulate.

    small

  • 79

    95% ethanol only denatures ________.

    surface proteins

  • 80

    70% ethanol penetrates bacteria and kills them by doing this to their proteins.

    coagulate

  • 81

    Only small amounts of coagulate are produced by 40% ethanol because they are _______.

    too diluted

  • 82

    It denatures protein irreversibly by breaking disulfide bonds and reducing them to SH.

    reducing agents