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CC1 LECTURE DEAN > PROTEINS PART 1 > Flashcards

PROTEINS PART 1 Flashcards

1
Q
  • chief nitrogenous macromolecules of cellular structure and orgnization
A

PROTEINS

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2
Q

([?] of cell’s dry weight)

A

50 to 70%

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3
Q

4 major elements found in proteins

A

Carbon, hydrogen, oxygen, nitrogen

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4
Q

Building blocks of proteins

A

Amino acids

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5
Q
  • consists of a definite number of amino acids arranged in a specific sequence
A

PROTEINS

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6
Q

PROTEINS PH

A

amphoteric

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7
Q
  • basic/alkaline; negative
A

amino group

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8
Q
  • acidic; positive
A

carboxyl

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9
Q
  • refers to the identity and specific order of amino acids in the polypeptide chain (amino acid sequence)
A

Primary structure

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10
Q
  • determine the overall shape of the protein
A

Primary structure

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11
Q

Arrangement of amino acids in a polypeptide chain

A

Primary structure

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12
Q

Each circle represents

A

one amino acid

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13
Q

free amino acid group

A

(N-terminal)

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14
Q

free carboxyl group

A

(C-terminal)

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15
Q

Result in biuret test: copper sulfate attaches to the peptide linkage = violet color

A

peptide bond

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16
Q

Primary structure linkage

A

peptide bond

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17
Q

Secondary structure linkage

A

hydrogen bonds

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18
Q

Tertiary structure linkage

A

covalent disulfide bond

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19
Q

Quaternary structure linkage

A

none

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20
Q

strong bond

A

covalent disulfide bond

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21
Q

conformation of the segments of polypeptide chain

A

Secondary structure

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22
Q

intramolcular folding of the polypeptide chain into a compact 3-dimenional structure

A

Tertiary structure

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23
Q

association of several polypeptide chains into larger “oligomeric” aggregate unit

A

Quaternary structure

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24
Q

Secondary structure shapes

A

a. alpha-helix and
b. beta-pleated sheets
c. random coils

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25
Q

Each amino groups have R groups/side chains that interact to one another = 3D STRUCTURE

A

Bending and folding

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26
Q

Separate polypeptide units are bended and folded

A

oligomeric

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27
Q

Several polypeptide units

A

oligomeric

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28
Q

Hemoglobin has four polypeptide units

A

Quaternary structure

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29
Q

2 alpha and 2 beta and Conjugated protein

A

Quaternary structure

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30
Q

A nonprotein (heme) combined with a protein molecule

A

Hemoglobin

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31
Q

ultimate product of digestion are amino acids

A

Simple

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32
Q

the protein molecule is combined with a non-protein component

A

Conjugated

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33
Q
  • a pigment is combined with a protein molecule
A

chromoprotein

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34
Q
  • a carbohydrate is combined with a protein molecule
A

glycoprotein

35
Q
  • a lipid is combined with a protein molecule
A

lipoprotein

36
Q

AA used for formation of new proteins

A

Repair body tissues

37
Q

non-protein coagulation factor

A

calcium

38
Q

protein coagulation factor

A

fibrinogen

39
Q

Important in blood coagulation and immunologic function

A

immunoglobulins

40
Q

For transport of metabolic substances

A

albumin, transferrin

41
Q

Maintenance of osmotic pressure

A

albumin

42
Q

preventing rx with acids

A

Maintenance of blood pH (buffers)

43
Q

neutralizes a system

A

Maintenance of blood pH (buffers)

44
Q

prevents significant changes in the pH

A

Maintenance of blood pH (buffers)

45
Q

Ex. Hemoglobin, Bicarbonate system

A

Maintenance of blood pH (buffers)

46
Q

Biocatalysts

A

enzymes

47
Q

increase protein synthesis

A

GH, Insulin, Thyroid hormone

48
Q

increase protein catabolism/breakdown

A

Glucocorticoids and Glucagon

49
Q

Thyroid hormone ex

A

T3 [triiodothyronine] and T4 [thyroxine])

50
Q

Glucocorticoids ex

A

Cortisol

51
Q

Protein digestion:

A

Polypeptides
Shorter peptides
Amino acids [ultimate product of protein digestion]
amino group enters the Kreb’s Henseleit cycle
Urea [ultimate product of protein digestion]

52
Q

amino group enters the [?]

A

Kreb’s Henseleit cycle

53
Q

[ultimate product of protein digestion]

A

Amino acids

54
Q

[ultimate product of catabolism]

A

Urea

55
Q

MAJOR PLASMA PROTEINS

A
  1. PRE-ALBUMIN
  2. ALBUMIN
  3. GLOBULINS
56
Q

I. Alpha1-globulins

A

a. α-1-antitrypsin
b. α-1-fetoprotein
c. α-1-Acid Glycoprotein (orosomucoid)

57
Q

II. Alpha2-globulins

A

A. Haptoglobin
B. Ceruloplasmin

58
Q

prouces albumin, a-1, a-2, B-globulins and fibrinogen

A

liver

59
Q

produces gamma globulin

A

reticuloendothelial

60
Q

groups are acc to their ELECTROPHORETIC MIGRATION

A

PRE-ALBUMIN

61
Q

largest protein fraction (52 to 62%)

A

ALBUMIN

62
Q

synthesized in the liver at a rate that is dependent on protein intake

A

ALBUMIN

63
Q
  • regulator of osmotic pressure
A

ALBUMIN

64
Q
  • negative acute phase reactant
A

ALBUMIN

65
Q

conc decrease in the presence of inflamation =

A

HYPOALBUMINEMIA

66
Q

– no clinical significance

A

HYPERALBUMINEMIA

67
Q

– hemoconcentration or dehydration

A

HYPERALBUMINEMIA

68
Q

– impaired synthesis (1 = liver disease; 2 = diminished protein intake)

A

HYPOALBUMINEMIA

69
Q

– malaborption or malnutrition

A

HYPOALBUMINEMIA

70
Q

– malaborption or malnutrition spp

A

(Capilliaria philippinensis)

71
Q

: loses urine through the kidneys

A

Nephrotic syndrome

72
Q
  • increased catabolism due to tissue damage and inflammation
A

ALBUMIN

73
Q

normal A/G ratio : 1.3 – 3 : 1

A

GLOBULINS

74
Q

(decreased plasma albumin)

A

low A/G ratio

75
Q

liver diseases, infectious diseases, multiple myeloma, nephritis

A

low A/G ratio

76
Q

Designates the electrophorotic migration

A

Alpha1-globulins

77
Q
  • complexes with trypsin in blood to inactivate it
A

α-1-antitrypsin

78
Q
  • increased in amniotic fluid and maternal serum in a neural tube defects (spina bifida)
A

α-1-fetoprotein

79
Q
  • liver tumor marker (liver carcinoma)
A

α-1-fetoprotein

80
Q
  • decreased in maternal serum during pregnancy associated with Down’s Syndrome
A

α-1-fetoprotein

81
Q
  • binds free hemoglobin
A

Haptoglobin

82
Q

contain peptide chains that on hydrolysis yield only AA

A

Simple

83
Q

may be fibrous or granular

A

Simple

84
Q

protein (apoprotein) + nonprotein (prosthetic group)

A

Conjugated

CC1 LECTURE DEAN (14 decks)

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