myoglobin located
muscle tissue cardiac and skkeletal
myoglobin functions
transports o2 from hemoglobin to mitochondria
storage for oxygen
heme group
prosthetic group found in both hemoglobin and myoglobin
heme group function
allows protiens to bind to oxygran
number of heme group sin myoglobin
1 heme group
number of myoglobins in hemoglobins
4
heme group spcial fetaure that allows in to bind to oxygen
contains fe 3+
similarities between myoglobin and hemoglobin
2,3 structure
same heme prosthetic group
oxygen transport
differences between myoglobin and hemoglobin
prmary structures
location
o2 affinity
myoglobin subunit
monomer
hemoglobin subunit
tetramer
variant amino acids
can be replaced with no changes
conserved amino acids
can be replaced with similar ones and no changes will occur
invariant
cannot be changed or else it will cause chage in sturcutre and fuction
hemoglobin pirmary strucutre
sequence of amino acids
hemoglobin seocndary structure
alpha helices
hemoglobin tertiery
side chain interactions with each subunit
quaternary
2 alpha 2 beta subunits
coopertivity
when protien completely changes its shape after binding
myoglobin coopertivity
does not occur
hemoglobin coopertivity
does occur
hemoglobin conformations
tense and relaxed
tense state in hemoglobin
deoxy
low o2
tissues
relaxed state in hemo
oxy
high o2 affinity
lungs