Talk:Myoglobin
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Article Grading: The following comments were left by the quality and importance raters: (edit · history · refresh · how to use this template) An expansion request have been made for this (certainly too short) article. – ClockworkSoul 16:28, 10 December 2006 (UTC) |
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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???? —Preceding unsigned comment 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)
[edit] Is it possible to remove the porphyrin from myoglobin.
I would like to know if anyone has a method to remove the porphyrin group from myoglobin in order to remove the colouring effect when cooking pelagic fish. —Preceding unsigned comment added by Laujensen (talk • contribs) 11:43, 10 September 2007 (UTC) I can tell you the lab method to remove the porfirin, you bring the solutin of Mb at a low pH~2 to unfold it and mix it w/ butanone, then separated the 2 phases. The porphyrine will bound with butanone(on the top) and mb will stay in the aquos solution (on the bottom). I know that to keep the red colour of meat you can bring it in N2 atmosphere so the Fe2+ doesn't oxidate. —Preceding unsigned comment added by 76.108.18.161 (talk) 21:13, 3 February 2008 (UTC)
[edit] new infobox
I know it was an imperfect merge with the new infobox, but I tried to preserve as much content as I could. Having said that, some information was lost. If people feel that the old infobox was superior, I'd be open to anything up to and including reverting back to the old version. AndrewGNF (talk) 02:06, 5 January 2008 (UTC)
