Talk:Myoglobin
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[edit] Question
This was posted by an anonymous user on the article's MCB comments:
- can anyone explain to me about fractional saturation associated with myoglobin???? —The preceding unsigned comment was added by 157.182.158.140 (talk • contribs) .
– ClockworkSoul 17:55, 21 September 2006 (UTC)
A discussion re: myoglobin involving fractional saturation may seem confusing as myoglobin only binds one oxygen molecule. The confusion should cease when one realises that a discussion of fractional saturation involves a number of myoglobin molecules. Therefore if we read a myoglobin saturation of 50%, this means that 50% of available myoglobin is saturated (has bound one oxygen molecule), not that one myoglobin molecule is 50% saturated (has bound half an oxygen molecule) which is impossible. Hope that helps. Mmoneypenny 11:14, 24 September 2006 (UTC) PS. Next time why not ask the Wiki reference desk, they're much better at this than I am.
[edit] Removed section
I removed this section from the article, because it seems to be a general description of the mechanism of protein folding, rather than anything specifically about myoglobin:
Myoglobin has eight helical segments connected by bends to form a compact, nearly spherical, tertiary structure. Myoglobin adopts the shape it does because of hydrophilic (water-loving) interactions of the polar side chains on acidic or basic amino acids. These acidic or basic amino acids with charged side chains tend to congregate on the exterior of the protein where they can be solvated by water. Those amino acids with neutral, non-polar side chains tend to congregate on the hydrocarbon-like interior of the protein molecule.
Adrian J. Hunter 15:04, 22 October 2006 (UTC)
