Extremophile
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== Positively charged myoglobin allows whales to hold their breaths during long dives == | == Positively charged myoglobin allows whales to hold their breaths during long dives == | ||
- | Whales dive and | + | Whales dive and swim the seas. Elephants, on the other hand, while gifted in memory, cannot hold their breaths long. One clue to this discrepancy is the difference in concentrations of <scene name='55/557585/Align_test/5'>myoglobin</scene> in whale and elephant muscle tissue: More myoglobin means more oxygen storage capacity, and 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. |
A very high concentration of myoglobin should lead to aggregation, which would prevent myoglobin from functioning, so how do whales' myoglobin deal with this extreme demand, and why can't elephants' myoglobin accumulate to high concentrations as well? In a recent article in the journal Science<ref>DOI:10.1126/science.1234192</ref>, the laboratories of Professors Berenbrink, Campbell, and Cossins demonstrate that ''natural variation in net positive charge explains aquatic and terrestrial animals' different diving abilities''. Following this pattern, 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 charge, where ''a protein with a higher net charge is much more soluble''. | A very high concentration of myoglobin should lead to aggregation, which would prevent myoglobin from functioning, so how do whales' myoglobin deal with this extreme demand, and why can't elephants' myoglobin accumulate to high concentrations as well? In a recent article in the journal Science<ref>DOI:10.1126/science.1234192</ref>, the laboratories of Professors Berenbrink, Campbell, and Cossins demonstrate that ''natural variation in net positive charge explains aquatic and terrestrial animals' different diving abilities''. Following this pattern, 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 charge, where ''a protein with a higher net charge is much more soluble''. |
Revision as of 17:54, 3 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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