JMS/sandbox22: Difference between revisions

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'''Molecular Tour:'''
'''Molecular Tour:'''


<scene name='58/585079/1u3d_magnet/2'>TextToBeDisplayed</scene> showing magnetic core in context of protein
Illia Solov'yov and Klau Schulten of the Theoretical and Computational Biophysics group at the University of Illinois at Urbana-Champaign think that the FAD factor and just several residues of a crytochrome protein is all it takes to register the magnetic field of the earth. The <scene name='58/585079/1u3d_magnet/2'>"magnetic core"</scene> they describe involves the <scene name='58/585079/1u3d_magnet/11'>FAD factor, three tryptophan residues, as well as the aspartic residues which neighbor the FAD factor</scene>. When light in the blue range hits the FAD factor it becomes excited, with the excitement diffused over its <scene name='58/585079/1u3d_magnet/10'>aromatic ring system</scene>. Then, one of the three neighboring aspartic acid residues donates a hydrogen proton from its hydroxyl group. The FAD factor then receives an electron from the neighboring tryptophan, from the tryptophan's nitrogen atom (shown in halo). The proton and electron that FAD received are attached to one of the nitrogen atoms on its ring (shown in halos). Next, this tryptophan received an electron from its <scene name='58/585079/1u3d_magnet/11'>neighboring tryptophan</scene>, and then the second tryptophan received an electron from its neighbor, a third tryptophan. Finally, the third tryptophan loses a proton to a neighboring element. At the end of this reaction, both the FAD factor and the third tryptophan residue contain a unpaired electron. The ability of the FAD factor to transfer back the electron received from the first trytophan to the third tryptophan is effected by the magnetic field of the Earth, because the two electons can exist in two spin states, parallel and antiparallel, with interconversion between states partly determined by the earth's magnetic force, and only the parallel state compatible with back transfer of the electron from FAD to trytophan. Thus, the speed which with FAD transfers back its donated electron is affected by the earth's magnetic field, and that speed can be registered by the brain as a proxy for where it lies relative to the earth's magnetic field.
<scene name='58/585079/1u3d_magnet/10'>TextToBeDisplayed</scene> no context
<scene name='58/585079/1u3d_magnet/11'>TextToBeDisplayed</scene> and now the core is in cpk.


<!-- <scene name='58/585079/1u3d_magnet/14'>TextToBeDisplayed</scene> superoxide interaction brings this to millisecond scale, which is the signaling scale. -->
<!-- <scene name='58/585079/1u3d_magnet/14'>TextToBeDisplayed</scene> superoxide interaction brings this to millisecond scale, which is the signaling scale. -->


<!--
'''Modest increase in net charge contributes about the same as the enormous difference in body mass to the maximum time underwater.  However''', a 3-fold increase in concentration of myoglobin ought to result in a similar fold increase in max time of breath holding, and the researchers show that body mass also makes a critical contribution to an animal's ability to hold its breath, with the overall equation for the contribution of body mass and myoglobin net charge as follows:
''log (maximum time underwater) = 0.223*log(body mass) + 0.972*log(myoglobin net charge) + 0.891''
As Asian elephant's weight is ~3K Kg, and a sperm whale's weight is ~50K Kg, it is clear that the modest increase in net charge contributes about the same as the enormous difference in body mass to the maximum time underwater.
-->
</StructureSection>
</StructureSection>



Revision as of 22:51, 13 May 2014

     

Extraordinary Proteins. Extreme lifestyles sometimes require

http://www.ks.uiuc.edu/Research/cryptochrome/



Elephants can hold their breath for 2 minutes, but whales can hold their breath for 90 minutes - and they do, migrating underwater around the world. To find out how, a group of researchers contacted museums and zoos around the world[1].



Molecular Tour:

Illia Solov'yov and Klau Schulten of the Theoretical and Computational Biophysics group at the University of Illinois at Urbana-Champaign think that the FAD factor and just several residues of a crytochrome protein is all it takes to register the magnetic field of the earth. The they describe involves the . When light in the blue range hits the FAD factor it becomes excited, with the excitement diffused over its . Then, one of the three neighboring aspartic acid residues donates a hydrogen proton from its hydroxyl group. The FAD factor then receives an electron from the neighboring tryptophan, from the tryptophan's nitrogen atom (shown in halo). The proton and electron that FAD received are attached to one of the nitrogen atoms on its ring (shown in halos). Next, this tryptophan received an electron from its , and then the second tryptophan received an electron from its neighbor, a third tryptophan. Finally, the third tryptophan loses a proton to a neighboring element. At the end of this reaction, both the FAD factor and the third tryptophan residue contain a unpaired electron. The ability of the FAD factor to transfer back the electron received from the first trytophan to the third tryptophan is effected by the magnetic field of the Earth, because the two electons can exist in two spin states, parallel and antiparallel, with interconversion between states partly determined by the earth's magnetic force, and only the parallel state compatible with back transfer of the electron from FAD to trytophan. Thus, the speed which with FAD transfers back its donated electron is affected by the earth's magnetic field, and that speed can be registered by the brain as a proxy for where it lies relative to the earth's magnetic field.


myoglobin (PDB entry 1u3d)

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References:References:

  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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Joseph M. Steinberger