Extremophile
From Proteopedia
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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/5'>classic myoglobin structure (default scene)</scene> | ||
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<scene name='55/557585/Align_test/18'>elephant's amino acids in yellow halos</scene> | <scene name='55/557585/Align_test/18'>elephant's amino acids in yellow halos</scene> | ||
| - | <scene name='52/523344/Elephantwhale/19'> | + | <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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The <scene name='55/557585/Align_test/5'>classic myoglobin structure (default scene)</scene> was solved by John Kendrew in the mid-1900s,and continues to be a classic in protein structure research. Myoglobin is a relatively small protein at 153 (sometimes 154) amino acids. The polypeptide <scene name='55/557585/Align_test/4'>chain simply folds over the heme ligand</scene>, cradling it between halves of the protein chain. But myoglobin research has revealed that proteins are dynamic: myoglobin the protein "breaths" in molecular imitation of our lungs movement, as it changes conformations to take up oxygen and release it. This is one example among many, of the contributions myoglobin has made to the structural biology field of research. | The <scene name='55/557585/Align_test/5'>classic myoglobin structure (default scene)</scene> was solved by John Kendrew in the mid-1900s,and continues to be a classic in protein structure research. Myoglobin is a relatively small protein at 153 (sometimes 154) amino acids. The polypeptide <scene name='55/557585/Align_test/4'>chain simply folds over the heme ligand</scene>, cradling it between halves of the protein chain. But myoglobin research has revealed that proteins are dynamic: myoglobin the protein "breaths" in molecular imitation of our lungs movement, as it changes conformations to take up oxygen and release it. This is one example among many, of the contributions myoglobin has made to the structural biology field of research. | ||
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[http://www.chem.utoronto.ca/coursenotes/GTM/JM/Mbstart.htm excellent myoglobin tutorial to complement proteopedia articles] | [http://www.chem.utoronto.ca/coursenotes/GTM/JM/Mbstart.htm excellent myoglobin tutorial to complement proteopedia articles] | ||
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</StructureSection> | </StructureSection> | ||
{{Reflist}} | {{Reflist}} | ||
Revision as of 20:07, 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
Proteopedia Page Contributors and Editors (what is this?)
Joseph M. Steinberger, Joel L. Sussman, Alexander Berchansky, Michal Harel
