問題一覧
1
chief constituents of skin, bones, hair, and nails. (collagen, keratin)
STRUCTURE
2
-chemical reactions in the body are catalyzed by proteins called enzymes.
CATALYSIS
3
-muscles are made up of protein called myosin and actin.
MOVEMENT
4
hemoglobin carries oxygen from the lungs and carbon dioxide from cells to the lungs.
TRANSPORT
5
includes insulin, erythropoietin, and human growth hormone.
HORMONES
6
the body produces antibodies to fight diseases.
fibrinogen is used in the formation of blood clot.
PROTECTION
7
casein in milk and ovalbumin in eggs store nutrients for newborn mammals and birds.
ferritin stores iron
STORAGE
8
control expression of genes
REGULATION
9
Two major types of proteins
fibrous proteins and globular proteins
10
these protein, the molecule are constituted by several coiled cross-linked
polypeptide chains, they are insoluble in water and highly resistant to enzyme
digestion. The ratio of length to breath (axial ratio) is more than 10 in such protein.
Fibrous proteins
11
the major protein of the connective tissue, insoluble in water,
acids or alkalis. But they are convertible to water-soluble gelatin, easily
digestible by enzymes.
Collagen
12
present in tendons, arteries and other elastic tissues, not convertible
to gelatin.
Elastins
13
protein of hair, nails etc.
Keratin
14
The building blocks of proteins
Amino Acids
15
Amino acids which are not synthesized in the body and must be provided in the diet to meet an animal’s metabolic needs are called essential amino acids.
Essential Amino Acids
16
These amino acids are need not be provided through diet, because they can be biosynthesized in adequate amounts within the organism.
Non-Essential Amino Acids
17
Compound formed when two amino acids linked by 1 peptide bond.
Examples:
Carnosine ( β-alanyl-L-histidine)
Anserine (β-alanyl-N-methylhistidine)
Aspartame (Asparagine-phenylalanine)
Dipeptides
18
Compound formed when three amino acids linked by 2 peptide bond.
Examples;
Glutathione ( Glutamyl-cystinyl-glycine)
Opthalmic acid (L-γ-Glutamyl-α-L-amino butyrl-glycine)
Tripeptides
19
Compound formed when more than 2 and less than 20 amino acids are linked by peptide bonds.
Examples;
Endomorphin-1 ( Tyrosine-proline-tryptophan-phenylalanine)
Oligopeptides
20
Compound formed when more than 20 amino acids are linked by peptide bond.
Examples:
Insulin
Growth hormone
Polypeptides
21
is amide linkage formed by the reaction between α-carboxyl group of one amino acid and α-amino group of another amino acid with the elimination of water molecule.
Peptide
22
Consists of the sequence of amino acids that makes up the chain.
PRIMARY STRUCTURE
23
a repetitive structure of the protein backbone.
SECONDARY STRUCTURE
24
a secondary structure where the protein folds into a coil held together by hydrogen bonds parallel to the axis of the coil.
Alpha- helix
25
the backbone of two protein chains in the same or different molecules is held together by hydrogen bonds.
Beta-pleated sheet
26
The complete 3-D arrangement of the atoms in proteins.
TERTIARY STRUCTURE
27
most often involved in stabilization of the tertiary structure of proteins is the disulfide bond.
Covalent Bond
28
tertiary structures are stabilized by ____ between polar groups on side chains or between side chains and the peptide backbone.
Hydrogen bonding
29
also called electrostatic attractions, occur between two amino acids with ionized side chains. That is between an acidic amino acid and a basic amino acid side chain.
Salt bridges
30
-in aqueous solutions, globular proteins usually turn their polar groups outward (toward the aqueous solvent), and their nonpolar groups inward, away from the water molecules. The nonpolar groups prefer to interact with each other.
Hydrophobic interactions
31
two sides with the same charge would normally repel each other, but they can also be linked via metal ion.
Metal ion coordination
32
the spatial relationship and interactions between subunits in a protein that has more than 1 polypeptide chain.
-determines how different subunits fit into an organized whole.
QUARTERNARY STRUCTURE
33
Hgb in adult is made of 4 chains (globins): 2 identical alpha chains of 141 amino acid residues each and two identical beta chains of 146 residues each.
Hemoglobin
34
the triple helix units, called tropocollagen, constitute the soluble form of collagen. They are stabilized by hydrogen bonding between the backbones of the 3 chains.
Collagen
35
the loss of the secondary, tertiary, and quaternary structures of a protein by a chemical or physical agent that leaves the primary structure intact.
Denaturation
36
Sequence of a chain of amino acids
Primary Protein Structure
37
Local folding of the polypeptide chain into helices or sheets
Secondary Protein Structure
38
Three- dimensional folding pattern of a protein due to side chain interactions
Tertiary Protein Structure
39
Protein consisting of more than one amino acid chain
Quarternary Protein Structure
40
This test gives positive results with proteins, peptides, amino acids and other primary amines, including ammonia. Proline and hydroxyproline give yellow color with ninhydrin, while other acids give blue
Ninhydrin Test
41
The ____ test for proteins qualitatively detects the presence of proteins in solution with the development of a deep violet color. In alkaline condition, ____ reacts with compounds containing two or more peptide bonds to form complexes of violet color
Biuret Test
42
test utilizes a nitration reaction which identifies the presence of activated benzene ring. The end product of this reaction is yellow in color and the name comes from Greek word ‘Xanthos’ meaning yellow. Aromatic groups of either the free amino acid or protein undergo nitration on
Xanthoproteic Test
43
is present in proteins as cystine, cysteine or methionine. In alkaline media, lead acetate reacts to form black colored precipitate.
Sulphur Test
44
test is specifically used for casein. On heating with concentrated nitric acid and concentrated sulfuric acid, casein is digested and phosphorous is released. NH3 is added to provide alkaline media.
Neuman’s Test
45
This method tests the presence of Tyrosine in the test sample.
Principle: The phenol group of tyrosine is nitrated by nitric acid. Then, this product forms a complex with mercury (I) and mercury (II) which gives pink to brick red color, to the solution.
Millon’s Test
46
Protein basis: Defective type I collagen.
•Signs & symptoms:
•Multiple bone fractures with minimal trauma
•Blue sclera (whites of the eyes look bluish)
•Hearing loss (abnormal ossicles)
•Dental problems (brittle teeth)
Osteogenesis Imperfecta (OI)
47
Protein basis: Collagen synthesis defect.
•Signs & symptoms:
•Hyperelastic (stretchy) skin
•Joint hypermobility (“double-jointed”)
•Easy bruising & fragile tissues
•Slow wound healing
Ehlers-Danlos Syndrome (EDS)
48
Protein basis: Defect in fibrillin-1 (structural glycoprotein).
Signs & symptoms:
•Tall, thin build with long arms, legs, and fingers (arachnodactyly)
•Lens dislocation in eyes
•Aortic aneurysm (risk of rupture)
Marfan Syndrome
49
Protein basis: Deficiency of phenylalanine hydroxylase.
•Signs & symptoms:
•Intellectual disability if untreated
•Seizures
•Musty or mousy odor of urine
•Light skin and hair (↓ melanin synthesis)
Phenylketonuria (PKU)
50
Protein basis: Deficiency of homogentisic acid oxidase.
•Signs & symptoms:
•Urine turns black on standing
•Arthritis (due to pigment deposition in joints)
•Dark pigmentation in cartilage and connective tissue (ochronosis)
Alkaptonuria
51
Protein basis: Deficiency of branched-chain ketoacid dehydrogenase.
•Signs & symptoms:
•Sweet, maple syrup-like odor in urine
•Poor feeding, vomiting in infants
•Seizures, developmental delay
Maple Syrup Urine Disease (MSUD)
52
Protein basis: Mutation in hemoglobin (HbS).
•Signs & symptoms:
•Fatigue, anemia
•Pain crises (due to blocked blood vessels)
•Swelling in hands/feet (dactylitis)
•Frequent infections
•Delayed growth
Sickle Cell Anemia
53
Protein basis: Reduced synthesis of hemoglobin chains.
•Signs & symptoms:
•Severe anemia (pallor, weakness)
•Bone deformities (frontal bossing, “chipmunk face”)
•Splenomegaly
•Growth retardation
Thalassemia
54
Protein basis: Defective ceruloplasmin → copper buildup.
Signs & symptoms:
•Liver cirrhosis (jaundice, abdominal swelling)
•Neurological issues (tremors, difficulty speaking)
•Psychiatric disturbances
•Kayser-Fleischer rings in the cornea
Wilson’s Disease
55
Protein basis: Excessive iron storage in ferritin/hemosiderin.
•Signs & symptoms:
oBronze skin pigmentation
oDiabetes mellitus (“bronze diabetes”)
oLiver cirrhosis
oJoint pain
Hemochromatosis
56
Protein basis: Misfolded amyloid proteins deposit in organs.
•Signs & symptoms:
oKidney disease (proteinuria, nephrotic syndrome)
oHeart problems (restrictive cardiomyopathy)
oNerve pain and weakness
Amyloidosis
57
Protein basis: Lack of insulin (protein hormone).
Signs & symptoms:
oPolyuria (frequent urination)
oPolydipsia (excessive thirst)
oPolyphagia (excessive hunger)
oWeight loss, fatigue
Diabetes Mellitus (Type 1)
58
Deficiency: Dwarfism (short stature, delayed growth).
Excess in children: Gigantism (abnormal height).
Excess in adults: Acromegaly (large hands, feet, jaw, thickened features).
Growth Hormone Abnormalities
59
Protein basis: Excess production of monoclonal immunoglobulins.
Signs & symptoms:
oBone pain, fractures
oAnemia, weakness
oKidney failure (Bence-Jones proteins in urine)
oRecurrent infections
Multiple Myeloma
60
Protein basis: Absent/defective B-cells → no antibodies.
Signs & symptoms:
oRecurrent bacterial infections (sinus, lungs, skin)
oSymptoms appear after maternal antibodies disappear (around 6 months old).
Agammaglobulinemia
61
Protein basis: Deposition of β-amyloid plaques and tau tangles.
Signs & symptoms:
oMemory loss
oConfusion, disorientation
oPersonality changes
Alzheimer’s Disease
62
Protein basis: Abnormal α-synuclein aggregation (Lewy bodies).
Signs & symptoms:
oTremors (shaking hands)
oMuscle stiffness
oSlow movements (bradykinesia)
oBalance problems
Parkinson’s Disease
63
Protein deficiency (adequate calories but poor protein).
•Signs & symptoms:
oEdema (swelling of legs/face)
oEnlarged fatty liver
oSkin and hair changes (depigmentation, reddish hair)
oIrritability
Kwashiorkor
64
Deficiency of both calories and protein.
Signs & symptoms:
oSevere wasting (skin and bones appearance)
oStunted growth
oWeakness, lethargy
oNo edema (unlike kwashiorkor)
Marasmus
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問題一覧
1
chief constituents of skin, bones, hair, and nails. (collagen, keratin)
STRUCTURE
2
-chemical reactions in the body are catalyzed by proteins called enzymes.
CATALYSIS
3
-muscles are made up of protein called myosin and actin.
MOVEMENT
4
hemoglobin carries oxygen from the lungs and carbon dioxide from cells to the lungs.
TRANSPORT
5
includes insulin, erythropoietin, and human growth hormone.
HORMONES
6
the body produces antibodies to fight diseases.
fibrinogen is used in the formation of blood clot.
PROTECTION
7
casein in milk and ovalbumin in eggs store nutrients for newborn mammals and birds.
ferritin stores iron
STORAGE
8
control expression of genes
REGULATION
9
Two major types of proteins
fibrous proteins and globular proteins
10
these protein, the molecule are constituted by several coiled cross-linked
polypeptide chains, they are insoluble in water and highly resistant to enzyme
digestion. The ratio of length to breath (axial ratio) is more than 10 in such protein.
Fibrous proteins
11
the major protein of the connective tissue, insoluble in water,
acids or alkalis. But they are convertible to water-soluble gelatin, easily
digestible by enzymes.
Collagen
12
present in tendons, arteries and other elastic tissues, not convertible
to gelatin.
Elastins
13
protein of hair, nails etc.
Keratin
14
The building blocks of proteins
Amino Acids
15
Amino acids which are not synthesized in the body and must be provided in the diet to meet an animal’s metabolic needs are called essential amino acids.
Essential Amino Acids
16
These amino acids are need not be provided through diet, because they can be biosynthesized in adequate amounts within the organism.
Non-Essential Amino Acids
17
Compound formed when two amino acids linked by 1 peptide bond.
Examples:
Carnosine ( β-alanyl-L-histidine)
Anserine (β-alanyl-N-methylhistidine)
Aspartame (Asparagine-phenylalanine)
Dipeptides
18
Compound formed when three amino acids linked by 2 peptide bond.
Examples;
Glutathione ( Glutamyl-cystinyl-glycine)
Opthalmic acid (L-γ-Glutamyl-α-L-amino butyrl-glycine)
Tripeptides
19
Compound formed when more than 2 and less than 20 amino acids are linked by peptide bonds.
Examples;
Endomorphin-1 ( Tyrosine-proline-tryptophan-phenylalanine)
Oligopeptides
20
Compound formed when more than 20 amino acids are linked by peptide bond.
Examples:
Insulin
Growth hormone
Polypeptides
21
is amide linkage formed by the reaction between α-carboxyl group of one amino acid and α-amino group of another amino acid with the elimination of water molecule.
Peptide
22
Consists of the sequence of amino acids that makes up the chain.
PRIMARY STRUCTURE
23
a repetitive structure of the protein backbone.
SECONDARY STRUCTURE
24
a secondary structure where the protein folds into a coil held together by hydrogen bonds parallel to the axis of the coil.
Alpha- helix
25
the backbone of two protein chains in the same or different molecules is held together by hydrogen bonds.
Beta-pleated sheet
26
The complete 3-D arrangement of the atoms in proteins.
TERTIARY STRUCTURE
27
most often involved in stabilization of the tertiary structure of proteins is the disulfide bond.
Covalent Bond
28
tertiary structures are stabilized by ____ between polar groups on side chains or between side chains and the peptide backbone.
Hydrogen bonding
29
also called electrostatic attractions, occur between two amino acids with ionized side chains. That is between an acidic amino acid and a basic amino acid side chain.
Salt bridges
30
-in aqueous solutions, globular proteins usually turn their polar groups outward (toward the aqueous solvent), and their nonpolar groups inward, away from the water molecules. The nonpolar groups prefer to interact with each other.
Hydrophobic interactions
31
two sides with the same charge would normally repel each other, but they can also be linked via metal ion.
Metal ion coordination
32
the spatial relationship and interactions between subunits in a protein that has more than 1 polypeptide chain.
-determines how different subunits fit into an organized whole.
QUARTERNARY STRUCTURE
33
Hgb in adult is made of 4 chains (globins): 2 identical alpha chains of 141 amino acid residues each and two identical beta chains of 146 residues each.
Hemoglobin
34
the triple helix units, called tropocollagen, constitute the soluble form of collagen. They are stabilized by hydrogen bonding between the backbones of the 3 chains.
Collagen
35
the loss of the secondary, tertiary, and quaternary structures of a protein by a chemical or physical agent that leaves the primary structure intact.
Denaturation
36
Sequence of a chain of amino acids
Primary Protein Structure
37
Local folding of the polypeptide chain into helices or sheets
Secondary Protein Structure
38
Three- dimensional folding pattern of a protein due to side chain interactions
Tertiary Protein Structure
39
Protein consisting of more than one amino acid chain
Quarternary Protein Structure
40
This test gives positive results with proteins, peptides, amino acids and other primary amines, including ammonia. Proline and hydroxyproline give yellow color with ninhydrin, while other acids give blue
Ninhydrin Test
41
The ____ test for proteins qualitatively detects the presence of proteins in solution with the development of a deep violet color. In alkaline condition, ____ reacts with compounds containing two or more peptide bonds to form complexes of violet color
Biuret Test
42
test utilizes a nitration reaction which identifies the presence of activated benzene ring. The end product of this reaction is yellow in color and the name comes from Greek word ‘Xanthos’ meaning yellow. Aromatic groups of either the free amino acid or protein undergo nitration on
Xanthoproteic Test
43
is present in proteins as cystine, cysteine or methionine. In alkaline media, lead acetate reacts to form black colored precipitate.
Sulphur Test
44
test is specifically used for casein. On heating with concentrated nitric acid and concentrated sulfuric acid, casein is digested and phosphorous is released. NH3 is added to provide alkaline media.
Neuman’s Test
45
This method tests the presence of Tyrosine in the test sample.
Principle: The phenol group of tyrosine is nitrated by nitric acid. Then, this product forms a complex with mercury (I) and mercury (II) which gives pink to brick red color, to the solution.
Millon’s Test
46
Protein basis: Defective type I collagen.
•Signs & symptoms:
•Multiple bone fractures with minimal trauma
•Blue sclera (whites of the eyes look bluish)
•Hearing loss (abnormal ossicles)
•Dental problems (brittle teeth)
Osteogenesis Imperfecta (OI)
47
Protein basis: Collagen synthesis defect.
•Signs & symptoms:
•Hyperelastic (stretchy) skin
•Joint hypermobility (“double-jointed”)
•Easy bruising & fragile tissues
•Slow wound healing
Ehlers-Danlos Syndrome (EDS)
48
Protein basis: Defect in fibrillin-1 (structural glycoprotein).
Signs & symptoms:
•Tall, thin build with long arms, legs, and fingers (arachnodactyly)
•Lens dislocation in eyes
•Aortic aneurysm (risk of rupture)
Marfan Syndrome
49
Protein basis: Deficiency of phenylalanine hydroxylase.
•Signs & symptoms:
•Intellectual disability if untreated
•Seizures
•Musty or mousy odor of urine
•Light skin and hair (↓ melanin synthesis)
Phenylketonuria (PKU)
50
Protein basis: Deficiency of homogentisic acid oxidase.
•Signs & symptoms:
•Urine turns black on standing
•Arthritis (due to pigment deposition in joints)
•Dark pigmentation in cartilage and connective tissue (ochronosis)
Alkaptonuria
51
Protein basis: Deficiency of branched-chain ketoacid dehydrogenase.
•Signs & symptoms:
•Sweet, maple syrup-like odor in urine
•Poor feeding, vomiting in infants
•Seizures, developmental delay
Maple Syrup Urine Disease (MSUD)
52
Protein basis: Mutation in hemoglobin (HbS).
•Signs & symptoms:
•Fatigue, anemia
•Pain crises (due to blocked blood vessels)
•Swelling in hands/feet (dactylitis)
•Frequent infections
•Delayed growth
Sickle Cell Anemia
53
Protein basis: Reduced synthesis of hemoglobin chains.
•Signs & symptoms:
•Severe anemia (pallor, weakness)
•Bone deformities (frontal bossing, “chipmunk face”)
•Splenomegaly
•Growth retardation
Thalassemia
54
Protein basis: Defective ceruloplasmin → copper buildup.
Signs & symptoms:
•Liver cirrhosis (jaundice, abdominal swelling)
•Neurological issues (tremors, difficulty speaking)
•Psychiatric disturbances
•Kayser-Fleischer rings in the cornea
Wilson’s Disease
55
Protein basis: Excessive iron storage in ferritin/hemosiderin.
•Signs & symptoms:
oBronze skin pigmentation
oDiabetes mellitus (“bronze diabetes”)
oLiver cirrhosis
oJoint pain
Hemochromatosis
56
Protein basis: Misfolded amyloid proteins deposit in organs.
•Signs & symptoms:
oKidney disease (proteinuria, nephrotic syndrome)
oHeart problems (restrictive cardiomyopathy)
oNerve pain and weakness
Amyloidosis
57
Protein basis: Lack of insulin (protein hormone).
Signs & symptoms:
oPolyuria (frequent urination)
oPolydipsia (excessive thirst)
oPolyphagia (excessive hunger)
oWeight loss, fatigue
Diabetes Mellitus (Type 1)
58
Deficiency: Dwarfism (short stature, delayed growth).
Excess in children: Gigantism (abnormal height).
Excess in adults: Acromegaly (large hands, feet, jaw, thickened features).
Growth Hormone Abnormalities
59
Protein basis: Excess production of monoclonal immunoglobulins.
Signs & symptoms:
oBone pain, fractures
oAnemia, weakness
oKidney failure (Bence-Jones proteins in urine)
oRecurrent infections
Multiple Myeloma
60
Protein basis: Absent/defective B-cells → no antibodies.
Signs & symptoms:
oRecurrent bacterial infections (sinus, lungs, skin)
oSymptoms appear after maternal antibodies disappear (around 6 months old).
Agammaglobulinemia
61
Protein basis: Deposition of β-amyloid plaques and tau tangles.
Signs & symptoms:
oMemory loss
oConfusion, disorientation
oPersonality changes
Alzheimer’s Disease
62
Protein basis: Abnormal α-synuclein aggregation (Lewy bodies).
Signs & symptoms:
oTremors (shaking hands)
oMuscle stiffness
oSlow movements (bradykinesia)
oBalance problems
Parkinson’s Disease
63
Protein deficiency (adequate calories but poor protein).
•Signs & symptoms:
oEdema (swelling of legs/face)
oEnlarged fatty liver
oSkin and hair changes (depigmentation, reddish hair)
oIrritability
Kwashiorkor
64
Deficiency of both calories and protein.
Signs & symptoms:
oSevere wasting (skin and bones appearance)
oStunted growth
oWeakness, lethargy
oNo edema (unlike kwashiorkor)
Marasmus