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BIOCHEM 2 - PROTEIN FUNCTION Flashcards

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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
secondary structure of myoglobin
2 Structure: Helical
26
tertiary structure of myoglobin
3 Structure: Globular
27
Found in skeletal and cardiac muscle
myoglobin
28
Folded globin chain forms a crevice which encloses a heme group
myoglobin
29
Heme group of myoglobin is inside the protein since it’s
hydrophobic
30
Roughly spherical molecule found in red blood cells
hemoglobin
31
Transport O2 from lungs to every tissue in the body
hemoglobin
32
Each globin chain of hemoglobin binds a heme group through the______ of a ____________
imidazole ring of a distal histidine residue
33
Globin of hemoglobin binds the heme at the (site)
5th site – “distal histidine site”
34
Tetramer: α2β2 | Each subunit contains one heme
hemoglobin
35
each subunit of hemoglobin contains how many heme
1 | total of 4 heme
36
how many heme does hemoglobin have
4
37
primary structure of hgb
``` α = 141 aa β = 146 aa ```
38
secondary structure of hgb
helical
39
tertiary structure of hgb
globular
40
quaternary structure of hgb
4 folded chain in tetrahedral arrangement
41
O2 and CO2 have different binding sites
Oxyhemoglobin Carbaminohemoglobin Carboxyhemoglobin Methemoglobin
42
Decrease in pH causes | 2
release of O2 and converts oxyhemoglobin to deoxyhemoglobin.
43
Genetically altered hemoglobin
sickle cell anemia
44
in sickle cell anemia which aa is defective
6th aa of β subunit | Glu Val
45
Regulatory proteins | Endocrine hormones
INSULIN & GLUCAGON
46
responsible for carbohydrate homeostasis
INSULIN & GLUCAGON
47
Produced from β-cells of Islets of Langerhans
INSULIN
48
regulatory protein with 2 polypeptide chain | (51 aa residues)
INSULIN
49
protein having | Intermolecular and intramolecular disulfide linkage
INSULIN
50
Hypoglycemic hormone
INSULIN
51
linkages found in insulin
Intermolecular and intramolecular disulfide linkage
52
Produced from α-cells of Islets of Langerhans
glucagon
53
Single polypeptide chain | (29 aa residues)
glucagon
54
Involved in increasing the blood levels of glucose
glucagon
55
how many aa residues are in a single polypeptide chain of glucagon
29 AA residues
56
how many aa residues are in insulin
51 AA residues
57
DISEASES RELATED TO INSULIN
Hypoglycemia Hyperglycemia Diabetes mellitus
58
Defense proteins | Also known as antibodies
immunoglobulins
59
secrete antibodies
B lymphocyte:
60
is a protein that is produced by the body in response to an “invading” (foreign) substance.
An antibody
61
- are produced as part of the body’s immune response to protect itself.
An antibody
62
is the substance that the body is trying to “fight off” (eliminate or reduce) by mounting an immune response
antigen
63
Y-shaped molecule | Tetramer
immunoglobulins
64
linkages found in immunoglobulins
Interchain and Intrachain disulfide linkages
65
chains of immunoglobulins
Light Chain | Heavy Chain
66
regions of immunoglobulins
Constant Region | Variable Region
67
Antibody that is commonly found in human secretions like tears, mucous and saliva
IgA
68
Cell attached antibody which function is still under study
IgD
69
Antibody responsible for allergic reactions
IgE
70
Most dominant antibody in humans. This antibody is responsible for secondary immune response
IgG
71
The antibody which serves as protection for primary infections
IgM
72
DISEASES related to immunoglobulins
Autoimmune Diseases Inherited Immunodeficiency HIV
73
In what oxidation state must the iron atom be for the heme to bind oxygen
Fe (II), +2
74
Which type of hemoglobin binds more tightly to oxygen, fetal or adult?
Fetal
75
is hemoglobin an allosteric enzyme
yes
76
the affinity of fetal hemoglobin for oxygen is higher than
that of maternal hemoglobin

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