chapter 5 biochem Flashcards

(29 cards)

1
Q

myoglobin located

A

muscle tissue cardiac and skkeletal

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

myoglobin functions

A

transports o2 from hemoglobin to mitochondria
storage for oxygen

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

heme group

A

prosthetic group found in both hemoglobin and myoglobin

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

heme group function

A

allows protiens to bind to oxygran

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

number of heme group sin myoglobin

A

1 heme group

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

number of myoglobins in hemoglobins

A

4

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

heme group spcial fetaure that allows in to bind to oxygen

A

contains fe 3+

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

similarities between myoglobin and hemoglobin

A

2,3 structure
same heme prosthetic group
oxygen transport

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

differences between myoglobin and hemoglobin

A

prmary structures
location
o2 affinity

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

myoglobin subunit

A

monomer

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

hemoglobin subunit

A

tetramer

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

variant amino acids

A

can be replaced with no changes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

conserved amino acids

A

can be replaced with similar ones and no changes will occur

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

invariant

A

cannot be changed or else it will cause chage in sturcutre and fuction

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

hemoglobin pirmary strucutre

A

sequence of amino acids

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

hemoglobin seocndary structure

A

alpha helices

17
Q

hemoglobin tertiery

A

side chain interactions with each subunit

18
Q

quaternary

A

2 alpha 2 beta subunits

19
Q

coopertivity

A

when protien completely changes its shape after binding

20
Q

myoglobin coopertivity

A

does not occur

21
Q

hemoglobin coopertivity

22
Q

hemoglobin conformations

A

tense and relaxed

23
Q

tense state in hemoglobin

A

deoxy
low o2
tissues

24
Q

relaxed state in hemo

A

oxy
high o2 affinity
lungs

25
bohr ph effect in tissues
cell resp. produces acid ph decrease hemo becomes tense o2 released
26
bohr ph effect in lungs
ph increase hemo shifts to relaxed o2 binds to hemo
27
bpg binding
only to tense hemo promotes o2 release aka decrease in affonty helps oxygen delivery to tissues
28
three types of cytoskeleton filaments
actin intermediate microtubules
29