Running Head: Sickle Cell Disease 1

Structure of Hemoglobin

Hemoglobin comprises about one-third of the mass of red blood cells in mammals(Touw, Joosten,

& Vriend, 2016). The transportation of oxygen from the lungs, through arteries to tissues, is the

primary function of hemoglobin and in addition to this, it helps in carrying back the carbon dioxide

back to the lungs through veins.

Protein Structure

Four polypeptide chains collectively form a molecule of hemoglobin. These polypeptide chains

include two beta chains of 146 amino acids and two alpha chains having 141 amino acid residues.

Very similar three-dimensional structures are formed by these two entirely different alpha and beta

chains with different amino acid sequences(Ruggiero Bachega et al., 2015). Non- covalent

interactions are used to hold this four chain together. Each of the chains comprises one heme group

that results in four binding sites for oxygen on the molecule of hemoglobin.

The 87th residue in the alpha chain is identified to be histidine F8 and 92nd residue in the beta chain

is identified to be histidine F8. Each of the four histidines has a heme group attached to it which

has an iron atom as well as an organic part on it. In the heme, the iron atom is used for biding the

four nitrogen in the central part of the protoporphyrin ring. The molecule of hemoglobin has a

spherical shape having a diameter of about 55 angstroms.

Structure of Beta goblin

Beta Goblin that also refers to HBB, β-globin or hemoglobin beta is identified to be a goblin

protein. This globin protein combined with the alpha goblin refers to HBA is responsible for

making the most common hemoglobin form in humans categorized as adults commonly known as
Sicke Cell Disease 2

HbA. The molecular weight of HbA is 15,867 Da and 146 amino acids long(González-Fernández

et al., 2015).

On the human Chromosome 11, HBB is encoded by the gene HBB. Numerous variants of proteins

are produced by the mutations in the gene that ultimately lead to numerous genetic disorders

including beta-thalassemia, sickle cell disorder and genetic resistance related to malaria in human

beings.
Sicke Cell Disease 3

References
González-Fernández, J., Daschner, A., Nieuwenhuizen, N. E., Lopata, A. L., De Frutos, C., Valls,

A., & Cuéllar, C. (2015). Haemoglobin, a new major allergen of Anisakis simplex.

International journal for parasitology, 45(6), 399-407.

https://www.researchgate.net/profile/Alvaro_Daschner/publication/272172262_Hemoglobin_a_n

ew_major_allergen_of_Anisakis_simplex/links/5662931108ae418a786a57ad/Hemoglobi

n-a-new-major-allergen-of-Anisakis-simplex.pdf

Ruggiero Bachega, J. F., Vasconcelos Maluf, F., Andi, B., D'Muniz Pereira, H., Falsarella

Carazzollea, M., Orville, A. M., . . . Horjales Reboredo, E. (2015). The structure of the

giant haemoglobin from Glossoscolex paulistus. Acta Crystallographica Section D:

Biological Crystallography, 71(6), 1257-1271.

http://repositorio.unicamp.br/bitstream/REPOSIP/235720/1/pmed_26057666.pdf

Touw, W. G., Joosten, R. P., & Vriend, G. (2016). New biological insights from better structure

models. Journal of molecular biology, 428(6), 1375-1393.

https://www.sciencedirect.com/science/article/pii/S0022283616000899