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SFM Block 1 > Globular Proteins > Flashcards

Globular Proteins Flashcards

1
Q

Describe structure of hemoglobin (HbA)

A

2 alpha subunits, 2 beta subunits
Each have a heme inside which has a Fe2+ inside and an O2 inside each

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2
Q

Oxygen bound hemoglobin

A

oxyhemoglobin

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3
Q

non oxygen bound hemoglobin

A

deoxyhemoglobin

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4
Q

CO2 bound hemoglobin

A

carbaminoglobin

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5
Q

what does Hydrogen bound hemoglobin create?

A

buffer

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6
Q

function of 2,3 BPG

A

regulates HbA affinity for Oxygen
binds on B subnunit for hemaglobin to unload Oxygen
Forces Oxygen unloading

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7
Q

CO2 in blood causes

A

release of ions, increase in acidity, decrease in pH and shift curve to the Right

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8
Q

Working muscle effect on oxygen hemoglobin dissociation curve

A

Goal is to send oxygen to the muscle (unload from hemoglobin)
decrease in pH, increase temperature, increase carbon dioxide, increase hydrogen concentration, increase 2,3 BPG (unloads Oxygen)
All causes shift right

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9
Q

Bohr effect

A

Hb affinity for oxygen decreases in tissue as there is an increase of CO2

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9
Q

Haldane effect

A

Hb affinity for CO2 decreases in lungs as increase in Oxygen

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10
Q

What does a left shift on the oxygen hemoglobin dissociation curve correlate to ?

A

higher affinity for oxygen
Does not want to let go

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11
Q

Fetal hemoglobin

A

much higher affinity for oxygen
alpha and gamma subunits

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12
Q

How to treat sickle cell disease?

A

gamma subunit of fetal hemaglobin injected, induce changes to blood from mutated B subunit

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13
Q

Myoglobin

A

No cooperativity in curve (one subunit)
final oxygen reserve for muscle, making it a high affinity for oxygen

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14
Q

globular protein characteristics

A

spherical, water soluble, catalytic/reg/transport in metabolic function
often contain heme

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15
Q

Myoglobin function

A

transport and store oxygen in skeletal and cardiac muscle cells

16
Q

hemoglobin function

A

transport oxygen, carbon dioxide, and hydrogen ions in red blood cells

17
Q

Structure of heme

A

4 rings goes from MP, MP, MP to PM (D ring shows orientation)

18
Q

Heme, CO and O2

A

CO much stronger in binding heme, creating asphyxiation
Overtime the CO binding weakens as is bent and allows Oxygen recovery

19
Q

Hemoglobin quarternary structure

A

between alpha and beta subunits, has hydrophobic interactions
Between dimers has polar bonds

20
Q

T form hemoglobin

A

tense, deoxygenated, tightly packed form with H bonds between dimers

21
Q

R form hemoglobin

A

relaxed, oxygenated, allow oxygen to enter with high affinity, poalr bonds rupture bewteeen dimers

22
Q

allosteric effects on the oxygen dissociation curve

A

partial pressure of Oxygen
pH
partial pressure of CO2
2,3 BPG
temperature

23
Q

Effect of CO2 in hemoglobin

A

10% carry as carbamate on Nterminal groups

can create T form of Hb and lead to right shift of curve as wants to offload oxygen

24
Q

binding of CO in hemoglobin

A

binds to Fe in heme shifting to R state making the tissue unable to release oxygen

25
Q

what chromosomes are important for organization of globin genes?

A

11 & 16

26
Q

hemoglobinopathies causes

A

decrease production of normal globin proteins
abnormal structure of one of globin chains of Hb molecule (decrease ability to bind oxygen)

27
Q

Hemoglobin S disease

A

HbS
red cell sickling, hemolytic anemia
Glutamic acid to valine
Screen in alkaline pH as migrate more slowly

28
Q

Hemoglobin C disease

A

HbC is variant of glutamic acid to lysine at position 6 of Beta chain

29
Q

Hemoglobin SC disease

A

compound of heterozygotes
significant red cell sickling

30
Q

methemoglobinemia

A

higher than normal level of methemoglobin
changes ferrous to ferric and decerases oxygen affinity

31
Q

Hepcidin

A

major regulator of ferroportin (exports Fe2+)

32
Q

important steps iron absorbtion

A

export of ferrous iron by ferroportin
oxidation of ferrous iron to ferric iron
load ferric iron onto transferrin
clear ferroportin from membrane by hepcidin

33
Q

Transferrin receptor (TfR1)

A

transmembrane glycoprotein
expresion incresaes when iron levels are low
allows Fe to enter cell

34
Q

iron deficiency anemia

A

microcytic hypochromic anemia
from chronic bleeding, malnutrition, or absorbtion disorder

SFM Block 1 (10 decks)

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