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Hemoglobin VS Myogolbin

by: Kirsten Duran

FUNCTIONS

Hemoglobin

Carries oxygen from the lungs to the rest of the body

Myoglobin

It stores oxygen in muscle cells, which can be utilized as energy.

Functions

structure

myoglobin- Has 153 amino acids

made up of four polypeptide chains-two alpha and two beta

Heterotetramer

Quaternary structure

Hemoglobin:: 141 amino acids

Monomer

Tertiary

there are made up of single polypeptide

structure

Background:

background

  • Hemoglobin and Myoglobin are heme protein that acts as oxygen binding protein
  • has 1 single subunit protein
  • Hemoglobin: is found all over the body.
  • Myoglobin: is found only in the Muscle tissue.
  • has 4 subunit protein

Factors:

factors

Iron associated with the heme binds oxygen. THe same iron found in the hemoglobin which gives its red color. this provides evrey hemoglobin molecule special capability to carry four oxygen molecules with it. when blood cells absorb oxygen color of blood changes to bright red, this why arteries carry bright red color blood, and vein that carry blood cells that are deoxygenated become dark red. The more hemoglobin in the blood cells means there more capacity to carry oxygen from the lungs to different organs of the body.

Myoglobin :

serves as a local oxygen reservoir that can temporairly provide oxygen when oxygenated blood delivery is insufficient during periods of intense muscular activity. iron within the heme group must be in the Fe2+ state to bind oxygen. If iron is oxidized to the Fe 3+ state, metmyoglobin is formed .

myoglobin

protein type

protein

Hemoglobin: it is a storgae protein

the quaternary structure of a hemoglobin molecule includes four tertiary structure protein chains, two of which are alpha helices and two of which are beta-pleated sheets.

myoglobin: it is a transport protein

myoglobin is a simple protein consisting of a single polypeptide. since the quaternary structure is composed of an assembly of subunits. Due to the lack of multiple subunits, it has the higest level of structure tertiary.

Affinity level:

  • Myogolobin: has a higher affinity fro oxygen because myoglobin is an oxygen storgae..

Hemoglobin is comparatively lower affinity to oxygen, can bind to CO2, CO and NO as well

Affinity level

prosthetic

Prosthetic

Heme of hemoglobin protein is a prosthetic group of hetero cyclic ring of porphyritic of an iron atom; the biological function of the group is for delivering oxygen to body tissue, such that bonding of ligand of gas molecules to the iron of the protein group changes the structure of the protein by amino acid group

Myoglobin is a monomeric oxygen-binding protein containing a heme prosthetic group. Myoglobin, whose physiological role is to facilitate diffusion in muscle, has a hyperbolic oxygen binding

Myoglobin

References:

References

Admin. (2022, January 4). Difference between hemoglobin and myoglobin. BYJUS. Retrieved March 29, 2022, from https://byjus.com/biology/differentiate-between-hemoglobin-and-myoglobin/#:~:text=Hemoglobin%20and%20myoglobin%20are%20heme,found%20only%20in%20muscle%20tissues.

Answer in molecular biology for Kylie #93790. Doing your Assignments. (2019, September 4). Retrieved March 29, 2022, from https://www.assignmentexpert.com/homework-answers/biology/molecular-biology/question-93790

Vanek, T. (2021, July 22). Biochemistry, myoglobin. StatPearls [Internet]. Retrieved March 29, 2022, from https://www.ncbi.nlm.nih.gov/books/NBK544256/#:~:text=Myoglobin%20facilitates%20oxygen%20diffusion.,bioactive%20nitric%20oxide%20to%20nitrate.

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