Extremophile
From Proteopedia
(Difference between revisions)
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- | <StructureSection load='1mbn' size='350' side='right' caption='myoglobin (PDB entry [[1mbn]])' scene='55/557585/Align_test/ | + | <StructureSection load='1mbn' size='350' side='right' caption='myoglobin - how the chain cradles the heme (PDB entry [[1mbn]])' scene='55/557585/Align_test/4'> |
== Extraordinary Proteins == | == Extraordinary Proteins == | ||
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== Extreme myoglobin allows whales and dolphins to dive and stay submerged for long periods of time== | == Extreme myoglobin allows whales and dolphins to dive and stay submerged for long periods of time== | ||
- | <ref>DOI:10.1126/science.1234192</ref> | ||
- | <scene name='55/557585/Align_test/5'>classic myoglobin structure (default scene)</scene> | ||
- | <scene name='55/557585/Align_test/4'>chain simply folds over the heme ligand</scene> | ||
- | <scene name='55/557585/Align_test/5'>classic protein</scene> | ||
- | <scene name='55/557585/Align_test/18'>elephant's amino acids in yellow halos</scene> | ||
- | <scene name='52/523344/Elephantwhale/19'>residue position 8</scene>, <scene name='52/523344/Elephantwhale/21'>12</scene>, <scene name='52/523344/Elephantwhale/22'>27</scene>, <scene name='52/523344/Elephantwhale/23'>34</scene>, <scene name='52/523344/Elephantwhale/24'>87</scene>, <scene name='52/523344/Elephantwhale/26'>116</scene>, <scene name='52/523344/Elephantwhale/27'>132</scene>, <scene name='52/523344/Elephantwhale/28'>140</scene>. | + | Whales dive and sail under oceans making heroic planetary circles. But elephants, while astonishing in their tight family structures and appreciation of mourning, cannot hold their breaths long. One clue to this discrepency is the difference in concentrations of <scene name='55/557585/Align_test/5'>myoglobin</scene> in whale and elephant muscle tissue: Whales have over ''15 times'' the concentration of myoglobin as elephants do (''70 mg/g'' wet mass compared to the elephants ''4.6''). But this leads to a biophysical question. |
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+ | A very high concentration of myoglobin should lead to aggregation, which would prevent myoglobin from functioning, so how do whales' myoglobin deal with this extraordinary demand, and why can't elephants' myoglobin accumulate to such high concentrations as well? In a fascinating article<ref>DOI:10.1126/science.1234192</ref>, Professor Micheal Berenbrink, Professor Andrew Cossins and collegues demonstrate that whale myoglobin has a net charge ''two formal charges higher'' than in elephants: ''+4 compared to +2'' in the elephant. '''Apparently a protein's solubility is a function of its net surface charge''', where '''a protein with a higher net charge is much more soluble'''. | ||
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+ | It all comes down to <scene name='55/557585/Align_test/18'>eight divergent amino acids (elephant's amino acids in yellow halos)</scene>. Without these amino acids, myoglobin in both whale and elephants has a charge of ''+1''. Calculate along the chain, in the N to C-terminal direction how just several amino acid switches bring the positive net charge of whale myoglobin up to ''+4'' and elephants to only ''+2'': <scene name='52/523344/Elephantwhale/19'>residue position 8</scene>, <scene name='52/523344/Elephantwhale/21'>12</scene>, <scene name='52/523344/Elephantwhale/22'>27</scene>, <scene name='52/523344/Elephantwhale/23'>34</scene>, <scene name='52/523344/Elephantwhale/24'>87</scene>, <scene name='52/523344/Elephantwhale/26'>116</scene>, <scene name='52/523344/Elephantwhale/27'>132</scene>, <scene name='52/523344/Elephantwhale/28'>140</scene>. | ||
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+ | Fascinating as this single example is, what is most intriguing in how this divergance in net positive charge explains the different diving abilities of aquatic verus terrestrial animals across the animal kingdom! | ||
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Revision as of 20:34, 2 December 2013
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- ↑ Mirceta S, Signore AV, Burns JM, Cossins AR, Campbell KL, Berenbrink M. Evolution of mammalian diving capacity traced by myoglobin net surface charge. Science. 2013 Jun 14;340(6138):1234192. doi: 10.1126/science.1234192. PMID:23766330 doi:http://dx.doi.org/10.1126/science.1234192
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Joseph M. Steinberger, Joel L. Sussman, Alexander Berchansky, Michal Harel