Structure of Haemoglobin: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
Haemoglobin is the oxygen binding protein found in red blood cells which also gives the blood cells their red colouration. The binding of oxygen to | Haemoglobin is the [[Oxygen|oxygen]] binding [[Protein|protein]] found in [[Red_blood_cells|red blood cells]] which also gives the blood cells their red colouration. The binding of oxygen to haemoglobin is related to its structure, and the rate of efficacy is further related to this. Haemoglobin found in [[mammal|mammals]] is composed of 4 subunits, and, thus, is known as tetrameric: they are further divided into 2 types: 2 are α, and 2 are β subunits <ref>Voet D., Voet J G., Pratt C W., (1999) Fundamentals of Biochemistry, New York: Wiley. Page 165</ref>. The [[quaternary structure|quaternary structure]] of haemoglobin changes upon it's binding of oxygen to maximise efficiency in areas of high [[p02|pO<sub>2</sub>]], and likewise the shape of haemoglobin changes when off-loading oxygen at areas of low pO<sub>2</sub>: this permits the delivery of the maximum amount of oxygen. Changes in shape include the rotation of the α<sub>1</sub>β<sub>1</sub> and α<sub>2</sub>β<sub>2</sub> dimers upon binding with oxygen; this change allows them to move with greater ease in order to deliver oxygen around the body <ref>Berg J., Tymoczko J. and Stryer L. (2007) Biochemistry, 6th edition, New York: WH Freeman. Page 210</ref> | ||
<references /> | <references /> | ||
<references /><br> | <references /><br> | ||
Revision as of 21:13, 8 December 2011
Haemoglobin is the oxygen binding protein found in red blood cells which also gives the blood cells their red colouration. The binding of oxygen to haemoglobin is related to its structure, and the rate of efficacy is further related to this. Haemoglobin found in mammals is composed of 4 subunits, and, thus, is known as tetrameric: they are further divided into 2 types: 2 are α, and 2 are β subunits [1]. The quaternary structure of haemoglobin changes upon it's binding of oxygen to maximise efficiency in areas of high pO2, and likewise the shape of haemoglobin changes when off-loading oxygen at areas of low pO2: this permits the delivery of the maximum amount of oxygen. Changes in shape include the rotation of the α1β1 and α2β2 dimers upon binding with oxygen; this change allows them to move with greater ease in order to deliver oxygen around the body [2]