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Botany > BIOCHEM 2 - PROTEIN FUNCTION > Flashcards

BIOCHEM 2 - PROTEIN FUNCTION Flashcards

1
Q

Most abundant protein in animals

A

collagen

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2
Q

SOLUBILITY OF COLLAGEN IN WATER

A

Water-insoluble fibers

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3
Q

Location of collagen in the cell

A

extracellular

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4
Q

Has great tensile strength (due to aldol crosslinks)

A

collagen

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5
Q

contributes to great tensile strength of collagen

A

aldol crosslinks

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6
Q

major role of collagen

A

stress-bearing component of connective tissues

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7
Q

location of collagen in body

A

Cartilage, bones, tendons, ligaments & skin

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8
Q

Primary Structure of collagen

A
  • (-X–Y–G-)-
    • X–Pro/Hyp; Y–any aa
    • each chain is about 800 aa residues long
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9
Q

Secondary Structure of collagen

A
  • Left-handed α-helix
    • 3.3 aa/turn
    • Pitch: 10 Å
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10
Q

Tertiary structure

A
  • 3 chains are parallel & wind each other in a right-handed manner to form a triple-helical structure
    • H-bond involving Hyp and Hyl residues
    • intramolecular and intermolecular aldol covalent crosslinks
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11
Q

Structural proteins

Found predominantly in walls of arteries, lungs, intestines and skins

A

elastin

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12
Q

“slide & stretch” over one another to maintain structural integrity and provide recoil

A

Elastin

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13
Q

MW of elastin

A

MW = 72 kDa;

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14
Q

hydrophobicity of elastin

A

highly hydrophobic

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15
Q

Connective tissue protein; has elastic properties

A

elastin

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16
Q

Consists predominantly of nonpolar aa residues, 1/3 G, 1/3 V + A, rich in P

A

elastin

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17
Q

protein having Random coil conformation

A

elastin

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18
Q

protein having Intramolecular and intermolecular desmosine crosslinks

A

elastin

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19
Q

is formed from threeallysyl side chainsplus one unalteredlysl side chain from the same or neighbouringpolypeptide.

A

Adesmosinecross-link

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20
Q

responsible for the rubber properties of elastin

A

Adesmosinecross-link

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21
Q

Hemeproteins; conjugated proteins

A

myoglobin

hemoglobin

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22
Q

Responsible to the red color of the blood
Prosthetic group (non-protein part)
Porphyrin ring
Centrally bound Fe+2

A

heme

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23
Q

Monomer

Contains a heme

A

myoglobin

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24
Q

primary structure of myoglobin

A

1 Structure: 153 aa

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25
Q

secondary structure of myoglobin

A

2 Structure: Helical

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26
Q

tertiary structure of myoglobin

A

3 Structure: Globular

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27
Q

Found in skeletal and cardiac muscle

A

myoglobin

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28
Q

Folded globin chain forms a crevice which encloses a heme group

A

myoglobin

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29
Q

Heme group of myoglobin is inside the protein since it’s

A

hydrophobic

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30
Q

Roughly spherical molecule found in red blood cells

A

hemoglobin

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31
Q

Transport O2 from lungs to every tissue in the body

A

hemoglobin

32
Q

Each globin chain of hemoglobin binds a heme group through the______ of a ____________

A

imidazole ring of a distal histidine residue

33
Q

Globin of hemoglobin binds the heme at the (site)

A

5th site – “distal histidine site”

34
Q

Tetramer: α2β2

Each subunit contains one heme

A

hemoglobin

35
Q

each subunit of hemoglobin contains how many heme

A

1

total of 4 heme

36
Q

how many heme does hemoglobin have

A

4

37
Q

primary structure of hgb

A 
α = 141 aa
β = 146 aa
38
Q

secondary structure of hgb

A

helical

39
Q

tertiary structure of hgb

A

globular

40
Q

quaternary structure of hgb

A

4 folded chain in tetrahedral arrangement

41
Q

O2 and CO2 have different binding sites

A

Oxyhemoglobin
Carbaminohemoglobin
Carboxyhemoglobin
Methemoglobin

42
Q

Decrease in pH causes

2

A

release of O2 and converts oxyhemoglobin to deoxyhemoglobin.

43
Q

Genetically altered hemoglobin

A

sickle cell anemia

44
Q

in sickle cell anemia which aa is defective

A

6th aa of β subunit

Glu Val

45
Q

Regulatory proteins

Endocrine hormones

A

INSULIN & GLUCAGON

46
Q

responsible for carbohydrate homeostasis

A

INSULIN & GLUCAGON

47
Q

Produced from β-cells of Islets of Langerhans

A

INSULIN

48
Q

regulatory protein with 2 polypeptide chain

(51 aa residues)

A

INSULIN

49
Q

protein having

Intermolecular and intramolecular disulfide linkage

A

INSULIN

50
Q

Hypoglycemic hormone

A

INSULIN

51
Q

linkages found in insulin

A

Intermolecular and intramolecular disulfide linkage

52
Q

Produced from α-cells of Islets of Langerhans

A

glucagon

53
Q

Single polypeptide chain

(29 aa residues)

A

glucagon

54
Q

Involved in increasing the blood levels of glucose

A

glucagon

55
Q

how many aa residues are in a single polypeptide chain of glucagon

A

29 AA residues

56
Q

how many aa residues are in insulin

A

51 AA residues

57
Q

DISEASES RELATED TO INSULIN

A

Hypoglycemia
Hyperglycemia
Diabetes mellitus

58
Q

Defense proteins

Also known as antibodies

A

immunoglobulins

59
Q

secrete antibodies

A

B lymphocyte:

60
Q

is a protein that is produced by the body in response to an “invading” (foreign) substance.

A

An antibody

61
Q
  • are produced as part of the body’s immune response to protect itself.
A

An antibody

62
Q

is the substance that the body is trying to “fight off” (eliminate or reduce) by mounting an immune
response

A

antigen

63
Q

Y-shaped molecule

Tetramer

A

immunoglobulins

64
Q

linkages found in immunoglobulins

A

Interchain and Intrachain disulfide linkages

65
Q

chains of immunoglobulins

A

Light Chain

Heavy Chain

66
Q

regions of immunoglobulins

A

Constant Region

Variable Region

67
Q

Antibody that is commonly found in human secretions like tears, mucous and saliva

A

IgA

68
Q

Cell attached antibody which function is still under study

A

IgD

69
Q

Antibody responsible for allergic reactions

A

IgE

70
Q

Most dominant antibody in humans. This antibody is responsible for secondary immune response

A

IgG

71
Q

The antibody which serves as protection for primary infections

A

IgM

72
Q

DISEASES related to immunoglobulins

A

Autoimmune Diseases
Inherited Immunodeficiency
HIV

73
Q

In what oxidation state must the iron atom be for the heme to bind oxygen

A

Fe (II), +2

74
Q

Which type of hemoglobin binds more tightly to oxygen, fetal or adult?

A

Fetal

75
Q

is hemoglobin an allosteric enzyme

A

yes

76
Q

the affinity of fetal hemoglobin for oxygen is higher than

A

that of maternal hemoglobin

Botany (324 decks)

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