Talk:Myoglobin

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Distal Prosthetic Group?[edit]

In section "Structure and Bonding" there is mention of "distal prosthetic group" which apparently refers to the distal histidine. Histidine is an amino acid of the protein, not a prosthetic group. Also, "picket fence porphyrin" is a particular organic-chemical analog of (sterically restrained?) heme, not the name of the hypothesis. Or am I missing something? Eaberry (talk) 19:54, 7 October 2012 (UTC)

Another Question[edit]

"Grilled meats can also take on a pink "smoke ring" that comes from the iron binding a molecule of carbon monoxide to give metmyoglobin." carbon monoxide bound myoglobin is MbCO, unbound oxidized myoglobin is metMB no?

Question[edit]

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 (talkcontribs)

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.

Removed section[edit]

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)

Seems reasonable to me. – ClockworkSoul 00:03, 23 October 2006 (UTC)

Is it possible to remove the porphyrin from myoglobin.[edit]

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 (talkcontribs) 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)

new infobox[edit]

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)

Problems with article[edit]

Article needs formatting and content editing by a qualified editor. Incomplete sentences exist and text is not formatted according to conventions used on Wikipedia. —Preceding unsigned comment added by 64.90.124.37 (talk) 01:14, 6 August 2008 (UTC)

Indeed. Looks like 117.197.162.104 (talk) clobbered a lot of the content through a series of edits. I considered rolling back the article to the last edit by Anonymi (talk · contribs) -- [1], but I also noticed that there's also something wrong with the earlier edit by ProteinBoxBot (talk · contribs) -- [2] (the protein box is messed up). Unfortunately, I don't know how to fix this latter problem, so I've rolled the article back to right before ProteinBoxBot's last edit. Noca2plus (talk) 05:44, 6 August 2008 (UTC)
I figured out the latter problem -- {{PBB/4151}} was corrupt. I fixed it and have included ProteinBoxBot's edit in the new version of the article. Noca2plus (talk) 18:17, 6 August 2008 (UTC)

Specificity of function[edit]

Would someone please clarify the specific functions of myoglobin in the human body and in other organism's bodies as well? Thank you. WinterSpw (talk) 03:06, 21 March 2010 (UTC)

How is Myoglobin formed?[edit]

I tried finding something on google but can't come up with anything The only possible result has a paywall Do we not know yet? —Preceding unsigned comment added by 66.49.133.217 (talk) 04:21, 2 November 2010 (UTC)

Main purpose of myglobin[edit]

It makes it seem like it needs to be put in the blood (following muscle injury). This is not its main purpose: it has oxygen, and exists already in muscle, so it can be used immediately 129.180.166.53 (talk) 10:12, 10 June 2012 (UTC)

almost all mammals[edit]

need a cite for this and, which mammals not Kelly222 (talk) 01:02, 14 June 2013 (UTC)