Haemoglobin Structure And Functions Flashcards
(11 cards)
Hemoglobin weighs………
64400 dalton
Haem constitute ……….. % of hemoglobin
4%
Globin 96%
Fe binds to ……… region of heme
F8 region
Fe in hemoglobin exist in …….. state
Ferrous
The hemoglobin chains are made up of ………… helical segments labelled
8 helical segment ls
A-H
Methemoglobin has………. amino acid in its F8 region
Tyrosine
In hemoglobin the orientation of the charged and uncharged molecule is
Charged molecules are oriented outside: lysine arginine, guanine
Uncharged in the hydrophobic core
In hemoglobin the orientation of the charged and uncharged molecule is
Charged molecules are oriented outside: lysine arginine, guanine
Uncharged in the hydrophobic core
Other oxygen carrying proteins are
Haemocyanin
Cholorocruonine
Hemerythrin
Vanabins
Erythrocruorin
Leg haemoglobin
Carbon dioxide is carried by haemoglobin as ………..
Carbaminohaemoglobin
Nitric oxide binds to what portion of the globin chain
Thiol group