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biochemistry Jonklaas > test 2: HB and Mb part 2 > Flashcards

test 2: HB and Mb part 2 Flashcards

1
Q

what is a protein family

A

evolutionaryily related proteins
globin fam

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2
Q

what does a hyperbola mean of cooperativity and sigmoidal

A

hyperbola = no cooperativity
sigmoidal = coopeativiity

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3
Q

what is the allosteric effect

A

binding at one site affects binding at others

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4
Q

how many subunits are required for allosterism

A

more than 1 subunit

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5
Q

what does the S curve indicate

A

allosterism

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6
Q

what is HOMOtropic allosteric interaction

A

effector and ligand are regulated by the same molecule
O2 and Hb

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7
Q

what is heterotropic allosteric interaction

A

effector and liganrd are differnt

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8
Q

what is an activator and what is an inhibitor

A
  • activator shifts the eq toward R state= positive interaction
    inhibitor shifts towards the T state meaning - interaction
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9
Q

descrube Hb oxugen affinity

A

starts out high but then FAVORS T state in the eq between T and R

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10
Q

what does BPg, h+ and co2 favor

A

tense low affinity

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11
Q

what are BPG,H+ and Co2 involved in

A

the Bohr effect

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12
Q

what does O2 favot

A

relaxed state

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13
Q

what is the bohr effect

A
  • increased temp = release of O2 from Hb
  • increase Co2, increase H+, increasing temp = release of O2 = decrease in affinity of H2
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14
Q

what happens to the curve if the affnity is decreased

A

curve shifts to the right

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15
Q

what happens withn
Temp increase
ph increase (basic)
co2 decrease

A

curve shifts to the left

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16
Q

how does temperature increase affect Hb affinity

A

high temp like fever will cause Yo2 to decrease wh

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17
Q

where on T state do Bohr protons bind

A
  • N terminal amino gprps and His 146 betal
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18
Q

what amino group is responsiblel for 2-30% of the bohr effect

A

N terminal amino groups

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19
Q

what happens to the pka during transition

A

changes the pka causing them to release coordinated H

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20
Q

how much does his 146 account for bohr effect

A

40

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21
Q

what protons ar released when Hb binds O2

A

H+ protons

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22
Q

where on the T state does CO2 bind

A

-N terminal amino groups and it can form carbamates
- not present in the R state

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23
Q

what metabolism is O2 apart of

A

aerobic

24
Q

oxidizing carbon cpds releases whawt

A

energy and O2 consume, CO2 is made

25
Q

is Co2 soluble in plasma

A

nowhat

26
Q

does cabonic anhydrase do

A

makes CO2 soluble by catalyzing the reaction

27
Q

how does carbonic anhydrse relate to pH

A

helps buffer blood at pH of 7.4

28
Q

how is carbonic anhydrase related to the bohr effecr

A
  • increases H+ conc bc CO2 is converted to bicarbonate
  • conformational changes stabilizing the tense (T state)
29
Q

what do the lungs facor

A

decrease H+, increase in pH = lungs = R state

30
Q

what do the capillaries favor

A
  • T state
  • high H+, low pH
31
Q

what is the most abundant organic phosphate in blood

A

2,3 BPG and it is made in glycolysis

32
Q

what does BPG do

A
  • binds to T state and stabilizes it
  • shifts equ. toward T STATe
33
Q

can BPG bind to the R state

A

no it can’t

34
Q

how is BPG helping with high altitude

A
  • body increse BPG decreased pO2
  • increase = more oxygen is being released to the tissues
35
Q

what does BPG do to Hb

A
  • gives Hb a p50 of 26 and without BPG it is 12 torr
  • fine tines Hb O2 binding capability ( without it O2 delivery would be bad)
36
Q

what other allosteric effector causes O2 to release

A

Cl-what

37
Q

what is the role of Cl-

A
  • netraulize the RBC electrosatic potential
  • binds to doexy Hb( causes O2 release) = chloride shift
38
Q

out of bPG, H+. CO2, Cl- and O2 what is the homotropic effector

A

O2

39
Q

what is the hill equation

A

E + nS = Es
E= enzme
S= substrate
n = number of S mlcls bound

40
Q

what does the farctional saturation ys =

A

bound total
n(Esn)/n(E+ESn)

41
Q

what does the slope of the hill coefficient show

A

the degree of cooperativity

42
Q

if n = 1. n>1, n<1

A
  1. n = 1 means non cooperative
    n>1 means positive coop
    n< 1 means negative coop
43
Q

for Hb what is cooperative

A

n is close to 3

44
Q

if 1 o2 binds…

A

the rest binds, and if 1 is released the rest are released

45
Q

what is the concerted model for allosteric proteins

A
  1. eq between t and r states
  2. ligand bind to either conform
  3. ligand absent = T state
  4. binding of ligand shifts toward R state
46
Q

what is a limiattion of the concerted model

A

only shows positive cooperativity

47
Q

what is the induced fit model

A
  • subinits can exits in T or R
  • presence of R = increased affnity
  • T to R is sequential process
  • accounts for both + and - cooperativity
48
Q

what are some effects of mutations on the protein

A
  • inheritable or genetic diseases
  • core of protein: affect the function and structure
49
Q

how can mutations be good for Hb

A
  • stabilize Metmoglobin like Hb boston
  • Fe+3 form is stabilized = O2 binding eliminated
    -cyanosis- blood is blue to chocolate brown
50
Q

describe pathological mutaions at surface of Hb

A
  • not as dangerous ‘
  • Hbe( glu 26 on beta chains turn to lys) no effect
51
Q

what can be a harfmul mutation

A
  • Hbs sickle cell anemia Glu6 on beta to val
52
Q

what is similar about HBs and HbA

A
  • same O2 binding
  • 4 hemes
    iron in Fe+2
    same active site
53
Q

Hbs pathology

A
  • E to V in beta chain making Hbs more hydrphobuc
  • ONLY IN T STATE( val fits into the pocket )
    linear polymers
54
Q

what happens when Hbs loses O2

A
  • Hbs starts to polymerize
  • polymersization causes blood cells to sickle
  • sickle = block capillaries and blood flow
55
Q

benefit of hBS gene

A
  • protection from maleria

biochemistry Jonklaas (8 decks)

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