Globin: Difference between revisions
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Globin is a [[Tertiary structure|tertiary]] protein that is found in [[Myoglobin|myoglobin]] and haemoglobin. Each globin molecule consist of 8 alpha helixes folded onto each other to make space to accommodate a [[Haem group|haem group]]<ref>Richard E Dickerson, Irving Geis. The structure and action of proteins. New York: Harper Row; 1969.Pages 44-51</ref>. myoglobin has 1 globin [[molecule|molecule]] whereas haemoglobin has four, two alpha and beta chains. Globin folds so that hydrophobic amino aids are on the inside and [[hydrophilic|hydrophilic]] one are on the inside, in this way they can prevent water oxidixing Fe(II), in the [[haem group|haem group]], to Fe(III)<ref>Richard E Dickerson, Irving Geis. The structure and action of proteins. New York: Harper Row; 1969. Pages 44-51</ref> | |||
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Latest revision as of 20:49, 3 December 2015
Globin is a tertiary protein that is found in myoglobin and haemoglobin. Each globin molecule consist of 8 alpha helixes folded onto each other to make space to accommodate a haem group[1]. myoglobin has 1 globin molecule whereas haemoglobin has four, two alpha and beta chains. Globin folds so that hydrophobic amino aids are on the inside and hydrophilic one are on the inside, in this way they can prevent water oxidixing Fe(II), in the haem group, to Fe(III)[2]