AA& PROTIENS Flashcards

(48 cards)

1
Q

What distinguishes proteins from carbohydrates and fats?

A

Presence of nitrogen (~16% of peptide chain)

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2
Q

What bond links amino acids together?

A

Peptide bond (covalent)

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3
Q

Define dipeptide, tripeptide, polypeptide

A

2 AA = dipeptide; 3 AA = tripeptide; many AA = polypeptide

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4
Q

Typical length of serum proteins

A

~100–150 amino acids

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5
Q

Primary protein structure

A

Amino acid sequence linked by covalent bonds

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6
Q

Secondary protein structure

A

Winding of polypeptide chain stabilized by hydrogen bonds

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7
Q

Tertiary protein structure

A

3D folding stabilized by disulfide bonds, H-bonds, electrostatic and hydrophobic interactions

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8
Q

Quaternary protein structure

A

Association of ≥2 polypeptide chains (e.g., hemoglobin)

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9
Q

Primary site of plasma protein synthesis

A

Liver (hepatocytes)

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10
Q

Two protein compartments

A

Intravascular and extravascular

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11
Q

Define nitrogen balance

A

Balance between protein anabolism and catabolism

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12
Q

Negative nitrogen balance occurs when

A

Catabolism > anabolism (burns, fever, starvation)

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13
Q

Positive nitrogen balance occurs when

A

Anabolism > catabolism (growth, pregnancy, recovery)

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14
Q

Enzyme deficiency in PKU

A

Phenylalanine hydroxylase

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15
Q

Accumulated substance in PKU

A

Phenylalanine → phenylpyruvic acid

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16
Q

Classic urine odor in PKU

A

Musty odor

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17
Q

PKU newborn screening test

A

Guthrie bacterial inhibition assay

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18
Q

MSUD enzyme defect

A

Keto acid decarboxylase deficiency

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19
Q

Amino acids affected in MSUD

A

Leucine, isoleucine, valine

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20
Q

MSUD hallmark clinical sign

A

Maple syrup/burnt sugar odor

21
Q

Enzyme deficient in homocystinuria

A

Cystathionine-β-synthase

22
Q

Elevated amino acids in homocystinuria

A

Homocysteine and methionine

23
Q

Major complications of homocystinuria

A

Thrombosis, osteoporosis, lens dislocation

24
Q

What reaction detects free amino acids?

A

Ninhydrin reaction (purple color)

25
Principle of the ninhydrin reaction
Free α-amino groups produce purple color proportional to concentration
26
Gold standard total protein method
Kjeldahl method
27
Biuret method principle
Cu²⁺ binds peptide bonds → violet color (540 nm)
28
Advantage of dye-binding methods
High sensitivity, easy to perform
29
Refractometry measures protein by
Change in refractive index
30
Major function of albumin
Maintains colloid osmotic pressure
31
Transport substances bound by albumin
Bilirubin, drugs, fatty acids, minerals
32
Albumin decreases in
Liver disease, malnutrition, muscle disorders
33
Albumin increases in
Dehydration
34
Prealbumin clinical significance
Sensitive marker of protein nutrition
35
Alpha-1 antitrypsin function
Inhibits trypsin; acute phase protein
36
Alpha-1 fetoprotein significance
Tumor marker for liver and germ cell cancer
37
Haptoglobin function
Binds free hemoglobin
38
Ceruloplasmin function
Copper transport; oxidation-reduction reactions
39
Disease associated with low ceruloplasmin
Wilson’s disease
40
Transferrin function
Iron transport protein
41
Transferrin increases in
Iron deficiency
42
C-reactive protein significance
Strong acute-phase inflammatory marker
43
pH used in serum protein electrophoresis
pH 8.6
44
Protein that migrates farthest toward anode
Albumin
45
Order of protein migration
Albumin → α1 → α2 → β → γ
46
Formula for globulin
Total protein − albumin
47
Decreased A/G ratio suggests
Liver disease with ↑ gamma globulins
48
A/G ratio formula
Albumin ÷ globulin