Monitoring of pre-frontal oxygen status in helicopter pilots using near-infrared spectrophotometers-4

Tes the downward head movement of the pilot (bold: 2~3 seconds, thin: 1~2 seconds).<p><b>Copyright information:</b></p><p>Taken from "Monitoring of pre-frontal oxygen status in helicopter pilots using near-infrared spectrophotometers"</p><p>http://www.dynamic-med.com/content/7/1/10</p><p>Dynamic Medicine : DM 2008;7():10-10.</p><p>Published online 11 Jul 2008</p><p>PMCID:PMC2503955.</p><p></p

Monitoring of pre-frontal oxygen status in helicopter pilots using near-infrared spectrophotometers-5

Indicates head down movement (1~2 seconds) of the pilot.<p><b>Copyright information:</b></p><p>Taken from "Monitoring of pre-frontal oxygen status in helicopter pilots using near-infrared spectrophotometers"</p><p>http://www.dynamic-med.com/content/7/1/10</p><p>Dynamic Medicine : DM 2008;7():10-10.</p><p>Published online 11 Jul 2008</p><p>PMCID:PMC2503955.</p><p></p

Monitoring of pre-frontal oxygen status in helicopter pilots using near-infrared spectrophotometers-1

Outline arrow indicates the downward head movement of the pilot (bold: 2~3 seconds, thin: 1~2 seconds).<p><b>Copyright information:</b></p><p>Taken from "Monitoring of pre-frontal oxygen status in helicopter pilots using near-infrared spectrophotometers"</p><p>http://www.dynamic-med.com/content/7/1/10</p><p>Dynamic Medicine : DM 2008;7():10-10.</p><p>Published online 11 Jul 2008</p><p>PMCID:PMC2503955.</p><p></p

Representative samples of oxy-hemoglobin (OHb) and deoxy-hemoglobin (HHb) changes in right and left frontal regions obtained from a subject during the head movement in laboratory measurement

<p><b>Copyright information:</b></p><p>Taken from "Monitoring of pre-frontal oxygen status in helicopter pilots using near-infrared spectrophotometers"</p><p>http://www.dynamic-med.com/content/7/1/10</p><p>Dynamic Medicine : DM 2008;7():10-10.</p><p>Published online 11 Jul 2008</p><p>PMCID:PMC2503955.</p><p></p

Functional importance of the oligomer formation of the cyanobacterial H+ pump Gloeobacter rhodopsin

Many microbial rhodopsins self-oligomerize, but the functional consequences of oligomerization have not been well clarified. We examined the effects of oligomerization of a H+ pump, Gloeobacter rhodopsin (GR), by using nanodisc containing trimeric and monomeric GR. The monomerization did not appear to affect the unphotolyzed GR. However, we found a significant impact on the photoreaction: The monomeric GR showed faint M intermediate formation and negligible H+ transfer reactions. These changes reflected the elevated pKa of the Asp121 residue, whose deprotonation is a prerequisite for the functional photoreaction. Here, we focused on His87, which is a neighboring residue of Asp121 and conserved among eubacterial H+ pumps but replaced by Met in an archaeal H+ pump. We found that the H87M mutation removes the "monomerization effects": Even in the monomeric state, H87M contained the deprotonated Asp121 and showed both M formation and distinct H+ transfer reactions. Thus, for wild-type GR, monomerization probably strengthens the Asp121-His87 interaction and thereby elevates the pKa of Asp121 residue. This strong interaction might occur due to the loosened protein structure and/or the disruption of the interprotomer interaction of His87. Thus, the trimeric assembly of GR enables light-induced H+ transfer reactions through adjusting the positions of key residues