test 2: HB and Mb part 2 Flashcards

1
Q

what is a protein family

A

evolutionaryily related proteins
globin fam

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what does a hyperbola mean of cooperativity and sigmoidal

A

hyperbola = no cooperativity
sigmoidal = coopeativiity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what is the allosteric effect

A

binding at one site affects binding at others

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

how many subunits are required for allosterism

A

more than 1 subunit

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what does the S curve indicate

A

allosterism

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

what is HOMOtropic allosteric interaction

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

what is heterotropic allosteric interaction

A

effector and liganrd are differnt

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

descrube Hb oxugen affinity

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

what does BPg, h+ and co2 favor

A

tense low affinity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what are BPG,H+ and Co2 involved in

A

the Bohr effect

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what does O2 favot

A

relaxed state

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

what happens to the curve if the affnity is decreased

A

curve shifts to the right

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

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

A

curve shifts to the left

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

how does temperature increase affect Hb affinity

A

high temp like fever will cause Yo2 to decrease wh

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

where on T state do Bohr protons bind

A
  • N terminal amino gprps and His 146 betal
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

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

A

N terminal amino groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

what happens to the pka during transition

A

changes the pka causing them to release coordinated H

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

how much does his 146 account for bohr effect

A

40

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

what protons ar released when Hb binds O2

A

H+ protons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

what metabolism is O2 apart of

24
Q

oxidizing carbon cpds releases whawt

A

energy and O2 consume, CO2 is made

25
is Co2 soluble in plasma
nowhat
26
does cabonic anhydrase do
makes CO2 soluble by catalyzing the reaction
27
how does carbonic anhydrse relate to pH
helps buffer blood at pH of 7.4
28
how is carbonic anhydrase related to the bohr effecr
- increases H+ conc bc CO2 is converted to bicarbonate - conformational changes stabilizing the tense (T state)
29
what do the lungs facor
decrease H+, increase in pH = lungs = R state
30
what do the capillaries favor
- T state - high H+, low pH
31
what is the most abundant organic phosphate in blood
2,3 BPG and it is made in glycolysis
32
what does BPG do
- binds to T state and stabilizes it - shifts equ. toward T STATe
33
can BPG bind to the R state
no it can't
34
how is BPG helping with high altitude
- body increse BPG decreased pO2 - increase = more oxygen is being released to the tissues
35
what does BPG do to Hb
- 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
what other allosteric effector causes O2 to release
Cl-what
37
what is the role of Cl-
- netraulize the RBC electrosatic potential - binds to doexy Hb( causes O2 release) = chloride shift
38
out of bPG, H+. CO2, Cl- and O2 what is the homotropic effector
O2
39
what is the hill equation
E + nS = Es E= enzme S= substrate n = number of S mlcls bound
40
what does the farctional saturation ys =
bound total n(Esn)/n(E+ESn)
41
what does the slope of the hill coefficient show
the degree of cooperativity
42
if n = 1. n>1, n<1
1. n = 1 means non cooperative n>1 means positive coop n< 1 means negative coop
43
for Hb what is cooperative
n is close to 3
44
if 1 o2 binds...
the rest binds, and if 1 is released the rest are released
45
what is the concerted model for allosteric proteins
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
what is a limiattion of the concerted model
only shows positive cooperativity
47
what is the induced fit model
- subinits can exits in T or R - presence of R = increased affnity - T to R is sequential process - accounts for both + and - cooperativity
48
what are some effects of mutations on the protein
- inheritable or genetic diseases - core of protein: affect the function and structure
49
how can mutations be good for Hb
- stabilize Metmoglobin like Hb boston - Fe+3 form is stabilized = O2 binding eliminated -cyanosis- blood is blue to chocolate brown
50
describe pathological mutaions at surface of Hb
- not as dangerous ' - Hbe( glu 26 on beta chains turn to lys) no effect
51
what can be a harfmul mutation
- Hbs sickle cell anemia Glu6 on beta to val
52
what is similar about HBs and HbA
- same O2 binding - 4 hemes iron in Fe+2 same active site
53
Hbs pathology
- E to V in beta chain making Hbs more hydrphobuc - ONLY IN T STATE( val fits into the pocket ) linear polymers
54
what happens when Hbs loses O2
- Hbs starts to polymerize - polymersization causes blood cells to sickle - sickle = block capillaries and blood flow
55
benefit of hBS gene
- protection from maleria