Extremophile

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 6: Line 6:
== 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 sail the seas, 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 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.
+
Whales dive and sail the seas. Elephants, however, while astonishing in their tight family structures, 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 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>, the laboratories of Professors Berenbrink, Campbell, and Cossins demonstrated 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'''.
+
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 the ''natural variation in net positive charge explains the 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''.
-
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>.
+
It 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 ''+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>.
*<span style="color:red">'''Asp and Glu'''</span> have a charge of ''-1'', <span style="color:blue">'''Arg and Lys'''</span> have a charge of ''+1'', <span style="color:lightblue">'''His'''</span> in the positions shown here - ''12'' and ''116'' (Table S2) - have a charge of about ''+0.5''.
*<span style="color:red">'''Asp and Glu'''</span> have a charge of ''-1'', <span style="color:blue">'''Arg and Lys'''</span> have a charge of ''+1'', <span style="color:lightblue">'''His'''</span> in the positions shown here - ''12'' and ''116'' (Table S2) - have a charge of about ''+0.5''.
-
Fascinating as this single example is, most intriguingly the authors show how this divergence in net positive charge explains the different diving abilities of aquatic versus terrestrial animals across the animal kingdom!
+
Intriguingly the authors show how this divergence in net positive charge explains the different diving abilities of aquatic versus terrestrial animals across the animal kingdom.
<!--
<!--

Revision as of 17:48, 3 December 2013

myoglobin - how the chain cradles the heme (PDB entry 1mbn)

Drag the structure with the mouse to rotate
  1. 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
Personal tools