JMS/sandbox22
Extraordinary Proteins. Extreme lifestyles sometimes require sensing the earth's magnetic field. Trytophan and aspartic acid residues may be key to an organism's ability to pick up where it is relative to the earth's poles. Birds, turtles, butterflies and other animals migrate with the help of the compasses built into their bodies. Little is known about the mechanistic nature of these compasses, and to fill the gap in knowledge, theoretical biophysicists Drs. Schulten and Solov'yov describe a nanomechanism within the birds' retina tissue, inside the rod cells, inside cryptochrome proteins known to process blue light for entraining circadian cycles, but now perhaps also deserving to be known as the seat of these organism's ability to sense magnetic fields. Molecular Tour: The cryptochrome protein obsorbs a single phton of blue light of 2.7 eV which excites an (the atoms involved in resonance are shown with halos). FAD is protonated by a (the proximate ones shown with halos), and the electron hole is filled through a series of electron transfers - a chain reaction involving three tryptophan amino acids (the nitrogen donators shown in halo) which form an extending from FAD in the interior to the surface of the protein. At this stage, FAD is in its active signalling state, and also the extra electron on FAD and lone electron on the final tryptophan amino acid (324) (location of the electron shown with halos). Klaus Schulten of the UIUC and Illia Solov'yov, now at the University of Southern Denmark, hypothesize 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 (the atoms involved in resonance are shown with halos). Then, one of the donates a hydrogen proton from its hydroxyl group (the proximate ones shown with halos). 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 with a halo). 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 this stage, the magnetic core contains an entangled pair of free radicals. The FAD factor contains a (shown with a halo), as does the third tryptophan residue on its donating nitrogen atom(shown with a halo).
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References:References:
- Cryptochrome and Magnetic Sensing, Theoretical and Computational Biophysics Group at the University of Illinois at Urbana-Champaign