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Haemoglobin

Haemoglobin. By Maja & Jonathan. Protein Functions. Iron-containing oxygen-transporting metallprotein Essential for respiration Located in all red blood cells of vertebrates Around 35% of our blood (including water) Four iron atoms; can bind up to four oxygen molecules

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Haemoglobin

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  1. Haemoglobin By Maja & Jonathan

  2. Protein Functions • Iron-containing oxygen-transporting metallprotein • Essential for respiration • Located in all red blood cells of vertebrates • Around 35% of our blood (including water) • Four iron atoms; can bind up to four oxygen molecules • Responsible for the red colour of blood (iron) • carries the oxygen from the lungs or gills to the cells

  3. History • Many people did research for Heamogobin • Discovered in 1840 by Hünefeld • Description of revisable oxygenation by Felix Hoppe-Seyler • 1959 Max Perutz determined protein structure; resulted in Nobel prize for Chemistry in 1962 • Role in blood determined by Claude Bernard

  4. Primary Structure • The haemoglobin  molecule consists of 4 polypeptide (globin) chains. In adults there are 2 alpha chains and 2 beta chains. • Peptide bond between each amino acidcalled residues

  5. Secondary Structure • Joined amino acid residues coil to form sections of alpha helix, which stabilizes the structure • Structure fairly compact

  6. TertiaryStructure • Mainbondinginvolvedin stabilising the structure of eachhaemoglobinchainis the attachment of a haemgroup  (a porphyrin ring containing iron) --->the yellowball on the picture • No disulphidebridgesinvolved in the tertiarystructure of haemoglobin.

  7. QuaternaryStructure • Twoalpha and two beta chainsareassociated to form a haemoglobinmolecule. • Morethan one peptidechain(multimericproteins). The manner in whichthesechainsfittogether (sort of like a puzzle) is the quaternarystructure.

  8. Defectivefunction • Sicklecellanaemia • In the primarystructure: a single alteration in the aminoacidstructure- substitution of  valineGTG (non polar) for glutamicacid GAG  (polar) - only in the beta chain - causes the molecule to packdifferentlyinto the red bloodcells, causingsickling. • Thalassemia • inheritedcondition in whichreducedproduction of one of the globin chainsoccurs. The unpairedotherchainbuildsup in the cells, resulting in problems.

  9. Works Cited • http://www.austincc.edu/emeyerth/tertiary.htm • http://faculty.stcc.edu/AandP/AP/AP2pages/Units18to20/blood/hemoglob.htm • http://www.biotopics.co.uk/as/haemoglobinproteinstructure.html

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