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Module 2 Part 2
100問 • 1年前
  • ユーザ名非公開
  • 通報

    問題一覧

  • 1

    Essential fatty acids are vital but are not synthesized in the body. Identify the essential fatty acids for humans.

    Linoleic acid (omega-6) and alpha-Linolenic acid (omega-3)

  • 2

    Which of the following is an omega-3 fatty acid?

    Alpha-linolenic acid

  • 3

    This carrier molecule transports activated fatty acids across the inner mitochondrial membrane.

    Carnitine

  • 4

    Lipids are biomolecules with diverse functions. Which of the following is true about lipids and lipid-derivatives?

    Eicosanoids act as messenger inside cells and between neighboring cells

  • 5

    Which of the following statements best describes fatty acid metabolism?

    The release of fatty acids and their subsequent beta-oxidation is a primary source of metabolic energy for the cell.

  • 6

    Determine the intermediate product formed in the biosynthesis of fatty acids, when malonyl-CoA reacts with Acetyl-CoA the product undergoes reduction and elimination of carbon dioxide.

    Butyryl-CoA

  • 7

    Number of mg of potassium hydroxide required to neutralize the free acids and hydrolyze the esters in 1g sample

    Saponification Value

  • 8

    Refers to the difference between saponification and acid value

    Ester Value

  • 9

    Number of mg of potassium hydroxide required to neutralize the acetic acid freed by the hydrolysis of acetylated fat

    Acetyl Value

  • 10

    Number of mg of potassium hydroxide required to neutralize the acid combined by acylation of the sample

    Hydroxyl Value

  • 11

    Measures the degree of unsaturation of the oil

    Iodine Value

  • 12

    Find the hormones used in the diagnosis of pancreatic disorders.

    Secretin and Gastrin

  • 13

    Analyze which oil is suitable for painting.

    Linseed oil

  • 14

    Hormone secreted by intestines

    Trypsin

  • 15

    Proteins are made up of a repertoire of ___ amino acids

    20

  • 16

    Functional groups of amino acids are

    Amino, Carboxyl acid

  • 17

    Amino acids are linked by ______________ to form polypeptide chains

    Peptide bonds

  • 18

    The peptide bond is not easily denatured and hydrolyzed

    True

  • 19

    The peptide bond is EASILY denatured and hydrolyzed

    False

  • 20

    This is the ONLY amino acid that has NO CHIRAL CENTER

    Glycine

  • 21

    This is the ONLY amino acid that is NOT OPTICALLY ACTIVE

    Glycine

  • 22

    Which amino acid has a phenol

    Tyrosine

  • 23

    Which amino acid has a phenyl

    Phenylalanine

  • 24

    Which amino acid has an indole ring

    Tryptophan

  • 25

    Tyrosine is converted to which of the following?

    Epinephrine, Norepinephrine, Dopamine

  • 26

    Brown pigment

    Melanin

  • 27

    Tyrosine is converted to which of the following?

    Melanin, Thyroxine

  • 28

    T4

    Thyroxine

  • 29

    Hormone that regulates sleep-wake pattern

    Melatonin

  • 30

    Tryptophan is converted to which of the following?

    Melatonin, Serotonin, Niacin

  • 31

    Melatonin

    Tryptophan

  • 32

    Melanin

    Tyrosine

  • 33

    Conversion of Glycine

    Heme

  • 34

    Non protein portion of Hemoglobin

    Heme

  • 35

    Enzyme for the conversion of Glutamate to GABA

    Glutamic Acid Decarboxylase

  • 36

    Intrachain Hydrogen Bonds

    Alpha Helix

  • 37

    Interchain Hydrogen Bonds

    Beta Sheets

  • 38

    The most important derivative of Glycosylated Hemoglobin

    HbA1C

  • 39

    Parameter used for monitoring blood glucose level

    HbA1C

  • 40

    Normal range of HbA1C

    6.9%

  • 41

    The major sugar derivative which is formed from the reaction of glucose with the amino terminal group on the beta subunit of hemoglobin

    HbA1C

  • 42

    Beta strands and alpha helices are amphipathic.

    Tertiary Structure

  • 43

    Protein that transport Oxygen

    Hemoglobin

  • 44

    Protein that transport most of the ACIDIC or NEUTRAL DRUGS

    Albumin

  • 45

    Casein from Milk

    Storage Proteins

  • 46

    Ovalbumin from Egg White

    Storage Proteins

  • 47

    PVT TIM HALL

    Essential Amino Acids

  • 48

    Hexokinase

    Catalytic Proteins

  • 49

    Ribonuclease

    Catalytic Proteins

  • 50

    Monoamine oxidase

    Catalytic Proteins

  • 51

    Myosin

    Contractile Proteins

  • 52

    Actin

    Contractile Proteins

  • 53

    Myosin

    Thick Filament

  • 54

    Actin

    Thin Filament

  • 55

    Collagen

    Structural Proteins

  • 56

    Keratin

    Structural Proteins

  • 57

    Elastin

    Structural Proteins

  • 58

    Structural protein of Skin and Cartillages

    Collagen

  • 59

    Defensive protein that is hemostatic plug

    Fibrin

  • 60

    Antibodies and Immunoglobulins

    Protective Proteins/ Defensive Proteins

  • 61

    Most common Immunoglobulins

    gamma-Globulin

  • 62

    MOST abundant in SERUM

    lgG

  • 63

    It is so small that it can crosses the placenta

    lgG

  • 64

    Main antibody in the PRIMARY response

    IgM

  • 65

    It is the LARGEST which is why it cannot cross the placenta

    IgM

  • 66

    Anamnestic

    Does not forget

  • 67

    Present in Secretions

    IgA

  • 68

    Prevents the attachment of bacteria and viruses in the mucous membranes (secretion glands)

    IgA

  • 69

    Colostrum

    Maternal Antibodies

  • 70

    Mediates TYPE 1 ALLERGIC REACTION

    IgE

  • 71

    Type I Allergic Mediators

    IgE

  • 72

    Type II Allergic Mediators

    IgG and IgM

  • 73

    Type III Allergic Mediators

    Ag-Ab complex mediator

  • 74

    Type IV Allergic Mediators

    T Cell mediator

  • 75

    A NONSPECIFIC immunoglobulin found on the surface of B cells where it acts as a receptor for antigens

    IgD

  • 76

    END PRODUCT OF metabolism OF PROTEINS

    Urea

  • 77

    Amino acids are classified based on their l side chains. Classify Glutamine and Aspartic acid.

    Carboxylic acid

  • 78

    Proteins are composed of monomer units called amino acids. The amino acids are linked together by __________ bonds.

    Peptide

  • 79

    Identify the chemical bond that joins amino acids together in a protein molecule.

    Peptide

  • 80

    What are the functional groups that are distinct amino acids?

    Amino acid and carboxylic acid groups

  • 81

    This is described as the simplest amino acid.

    Glycine

  • 82

    These are examples of transport and storage proteins:

    Hemoglobin, Myoglobin, serum Albumin

  • 83

    Ninhydrin Test is:

    Based on the reaction between the reagent and the amino group of the free amino acid of the test sample, which leads to the oxidation of the compound and its deamination, and resulting in the formation of a deep blue colored solution

  • 84

    The amino acid Tyrosine is converted to catecholamine. These are:

    Norepinephrine, epinephrine, dopamine

  • 85

    The most abundant of the serum immunoglobulins is:

    IgG

  • 86

    Among the 20 amino acids, which of the following pair undergoes non-oxidative direct deamination?

    Serine and Threonine

  • 87

    An amino acid relevant to the production of HEME

    Glycine

  • 88

    Protein Composition and Structure

    Proteins are built from a repertoire of 20 amino acids, The secondary structure of proteins refers to the conformation adopted by local regions of the polypeptide chain, The primary structure of proteins refer to the amino acid sequence.

  • 89

    The PRIMARY structure of Proteins

    Amino acids are linked by peptide bonds to form polypeptide chains.

  • 90

    The TERTIARY Structure of Proteins

    The tertiary structure describes the overall folding of the polypeptides chain, Many alpha helices and beta strands are amphipathic; that is, the alpha helix or beta strand has a hydrophobic face, which points into the protein interior, and a more polar face, which points into the solution, Pairing all the NH and CO groups by H-bonding is the secret of burying a segment of the main chain in a hydrophobic environment., The polypeptide chain folds so that its hydrophobic side chains are buried and its polar charged chains are on the surface

  • 91

    The secondary Structure of Proteins

    The secondary structure refer to the folded segments of alpha helices, beta strands, and turns that are formed by a regular pattern of H-bond between the peptide N-H and C=O groups of amino acids that are near one another in a linear sequence

  • 92

    Protein Beta Sheets

    The beta sheet is composed of 2 or more polypeptide chains called beta strands, Adjacent strands in a beta sheet can run in opposite directions or in the same direction, Beta sheets are more structurally diverse than alpha helices, Beta sheets are stabilized by H-bonding between polypeptide strands.

  • 93

    Fibrinogen

    Defensive

  • 94

    Collagen, Keratin

    Structural

  • 95

    MAO

    Catalytic

  • 96

    Hemoglobin

    Transport

  • 97

    Insulin

    Regulatory

  • 98

    Protein portion of an Enzyme

    Apoenzyme

  • 99

    Alpha Helix Breakers

    Proline, Glycine

  • 100

    Non Protein portion of an Enzyme

    Prosthetic group

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    問題一覧

  • 1

    Essential fatty acids are vital but are not synthesized in the body. Identify the essential fatty acids for humans.

    Linoleic acid (omega-6) and alpha-Linolenic acid (omega-3)

  • 2

    Which of the following is an omega-3 fatty acid?

    Alpha-linolenic acid

  • 3

    This carrier molecule transports activated fatty acids across the inner mitochondrial membrane.

    Carnitine

  • 4

    Lipids are biomolecules with diverse functions. Which of the following is true about lipids and lipid-derivatives?

    Eicosanoids act as messenger inside cells and between neighboring cells

  • 5

    Which of the following statements best describes fatty acid metabolism?

    The release of fatty acids and their subsequent beta-oxidation is a primary source of metabolic energy for the cell.

  • 6

    Determine the intermediate product formed in the biosynthesis of fatty acids, when malonyl-CoA reacts with Acetyl-CoA the product undergoes reduction and elimination of carbon dioxide.

    Butyryl-CoA

  • 7

    Number of mg of potassium hydroxide required to neutralize the free acids and hydrolyze the esters in 1g sample

    Saponification Value

  • 8

    Refers to the difference between saponification and acid value

    Ester Value

  • 9

    Number of mg of potassium hydroxide required to neutralize the acetic acid freed by the hydrolysis of acetylated fat

    Acetyl Value

  • 10

    Number of mg of potassium hydroxide required to neutralize the acid combined by acylation of the sample

    Hydroxyl Value

  • 11

    Measures the degree of unsaturation of the oil

    Iodine Value

  • 12

    Find the hormones used in the diagnosis of pancreatic disorders.

    Secretin and Gastrin

  • 13

    Analyze which oil is suitable for painting.

    Linseed oil

  • 14

    Hormone secreted by intestines

    Trypsin

  • 15

    Proteins are made up of a repertoire of ___ amino acids

    20

  • 16

    Functional groups of amino acids are

    Amino, Carboxyl acid

  • 17

    Amino acids are linked by ______________ to form polypeptide chains

    Peptide bonds

  • 18

    The peptide bond is not easily denatured and hydrolyzed

    True

  • 19

    The peptide bond is EASILY denatured and hydrolyzed

    False

  • 20

    This is the ONLY amino acid that has NO CHIRAL CENTER

    Glycine

  • 21

    This is the ONLY amino acid that is NOT OPTICALLY ACTIVE

    Glycine

  • 22

    Which amino acid has a phenol

    Tyrosine

  • 23

    Which amino acid has a phenyl

    Phenylalanine

  • 24

    Which amino acid has an indole ring

    Tryptophan

  • 25

    Tyrosine is converted to which of the following?

    Epinephrine, Norepinephrine, Dopamine

  • 26

    Brown pigment

    Melanin

  • 27

    Tyrosine is converted to which of the following?

    Melanin, Thyroxine

  • 28

    T4

    Thyroxine

  • 29

    Hormone that regulates sleep-wake pattern

    Melatonin

  • 30

    Tryptophan is converted to which of the following?

    Melatonin, Serotonin, Niacin

  • 31

    Melatonin

    Tryptophan

  • 32

    Melanin

    Tyrosine

  • 33

    Conversion of Glycine

    Heme

  • 34

    Non protein portion of Hemoglobin

    Heme

  • 35

    Enzyme for the conversion of Glutamate to GABA

    Glutamic Acid Decarboxylase

  • 36

    Intrachain Hydrogen Bonds

    Alpha Helix

  • 37

    Interchain Hydrogen Bonds

    Beta Sheets

  • 38

    The most important derivative of Glycosylated Hemoglobin

    HbA1C

  • 39

    Parameter used for monitoring blood glucose level

    HbA1C

  • 40

    Normal range of HbA1C

    6.9%

  • 41

    The major sugar derivative which is formed from the reaction of glucose with the amino terminal group on the beta subunit of hemoglobin

    HbA1C

  • 42

    Beta strands and alpha helices are amphipathic.

    Tertiary Structure

  • 43

    Protein that transport Oxygen

    Hemoglobin

  • 44

    Protein that transport most of the ACIDIC or NEUTRAL DRUGS

    Albumin

  • 45

    Casein from Milk

    Storage Proteins

  • 46

    Ovalbumin from Egg White

    Storage Proteins

  • 47

    PVT TIM HALL

    Essential Amino Acids

  • 48

    Hexokinase

    Catalytic Proteins

  • 49

    Ribonuclease

    Catalytic Proteins

  • 50

    Monoamine oxidase

    Catalytic Proteins

  • 51

    Myosin

    Contractile Proteins

  • 52

    Actin

    Contractile Proteins

  • 53

    Myosin

    Thick Filament

  • 54

    Actin

    Thin Filament

  • 55

    Collagen

    Structural Proteins

  • 56

    Keratin

    Structural Proteins

  • 57

    Elastin

    Structural Proteins

  • 58

    Structural protein of Skin and Cartillages

    Collagen

  • 59

    Defensive protein that is hemostatic plug

    Fibrin

  • 60

    Antibodies and Immunoglobulins

    Protective Proteins/ Defensive Proteins

  • 61

    Most common Immunoglobulins

    gamma-Globulin

  • 62

    MOST abundant in SERUM

    lgG

  • 63

    It is so small that it can crosses the placenta

    lgG

  • 64

    Main antibody in the PRIMARY response

    IgM

  • 65

    It is the LARGEST which is why it cannot cross the placenta

    IgM

  • 66

    Anamnestic

    Does not forget

  • 67

    Present in Secretions

    IgA

  • 68

    Prevents the attachment of bacteria and viruses in the mucous membranes (secretion glands)

    IgA

  • 69

    Colostrum

    Maternal Antibodies

  • 70

    Mediates TYPE 1 ALLERGIC REACTION

    IgE

  • 71

    Type I Allergic Mediators

    IgE

  • 72

    Type II Allergic Mediators

    IgG and IgM

  • 73

    Type III Allergic Mediators

    Ag-Ab complex mediator

  • 74

    Type IV Allergic Mediators

    T Cell mediator

  • 75

    A NONSPECIFIC immunoglobulin found on the surface of B cells where it acts as a receptor for antigens

    IgD

  • 76

    END PRODUCT OF metabolism OF PROTEINS

    Urea

  • 77

    Amino acids are classified based on their l side chains. Classify Glutamine and Aspartic acid.

    Carboxylic acid

  • 78

    Proteins are composed of monomer units called amino acids. The amino acids are linked together by __________ bonds.

    Peptide

  • 79

    Identify the chemical bond that joins amino acids together in a protein molecule.

    Peptide

  • 80

    What are the functional groups that are distinct amino acids?

    Amino acid and carboxylic acid groups

  • 81

    This is described as the simplest amino acid.

    Glycine

  • 82

    These are examples of transport and storage proteins:

    Hemoglobin, Myoglobin, serum Albumin

  • 83

    Ninhydrin Test is:

    Based on the reaction between the reagent and the amino group of the free amino acid of the test sample, which leads to the oxidation of the compound and its deamination, and resulting in the formation of a deep blue colored solution

  • 84

    The amino acid Tyrosine is converted to catecholamine. These are:

    Norepinephrine, epinephrine, dopamine

  • 85

    The most abundant of the serum immunoglobulins is:

    IgG

  • 86

    Among the 20 amino acids, which of the following pair undergoes non-oxidative direct deamination?

    Serine and Threonine

  • 87

    An amino acid relevant to the production of HEME

    Glycine

  • 88

    Protein Composition and Structure

    Proteins are built from a repertoire of 20 amino acids, The secondary structure of proteins refers to the conformation adopted by local regions of the polypeptide chain, The primary structure of proteins refer to the amino acid sequence.

  • 89

    The PRIMARY structure of Proteins

    Amino acids are linked by peptide bonds to form polypeptide chains.

  • 90

    The TERTIARY Structure of Proteins

    The tertiary structure describes the overall folding of the polypeptides chain, Many alpha helices and beta strands are amphipathic; that is, the alpha helix or beta strand has a hydrophobic face, which points into the protein interior, and a more polar face, which points into the solution, Pairing all the NH and CO groups by H-bonding is the secret of burying a segment of the main chain in a hydrophobic environment., The polypeptide chain folds so that its hydrophobic side chains are buried and its polar charged chains are on the surface

  • 91

    The secondary Structure of Proteins

    The secondary structure refer to the folded segments of alpha helices, beta strands, and turns that are formed by a regular pattern of H-bond between the peptide N-H and C=O groups of amino acids that are near one another in a linear sequence

  • 92

    Protein Beta Sheets

    The beta sheet is composed of 2 or more polypeptide chains called beta strands, Adjacent strands in a beta sheet can run in opposite directions or in the same direction, Beta sheets are more structurally diverse than alpha helices, Beta sheets are stabilized by H-bonding between polypeptide strands.

  • 93

    Fibrinogen

    Defensive

  • 94

    Collagen, Keratin

    Structural

  • 95

    MAO

    Catalytic

  • 96

    Hemoglobin

    Transport

  • 97

    Insulin

    Regulatory

  • 98

    Protein portion of an Enzyme

    Apoenzyme

  • 99

    Alpha Helix Breakers

    Proline, Glycine

  • 100

    Non Protein portion of an Enzyme

    Prosthetic group