4 research outputs found
Dynamic detection of electron spin accumulation in ferromagnet-semiconductor devices by ferromagnetic resonance
A distinguishing feature of spin accumulation in ferromagnet-semiconductor
devices is precession of the non-equilibrium spin population of the
semiconductor in a magnetic field. This is the basis for detection techniques
such as the Hanle effect, but these approaches become less effective as the
spin lifetime in the semiconductor decreases. For this reason, no electrical
Hanle measurement has been demonstrated in GaAs at room temperature. We show
here that by forcing the magnetization in the ferromagnet (the spin injector
and detector) to precess at the ferromagnetic resonance frequency, an
electrically generated spin accumulation can be detected from 30 to 300 K. At
low temperatures, the distinct Larmor precession of the spin accumulation in
the semiconductor can be detected by ferromagnetic resonance in an oblique
field. We verify the effectiveness of this new spin detection technique by
comparing the injection bias and temperature dependence of the measured spin
signal to the results obtained using traditional methods. We further show that
this new approach enables a measurement of short spin lifetimes (< 100 psec), a
regime that is not accessible in semiconductors using traditional Hanle
techniques.Comment: 4 figure
Structural and Mutational Analysis of Functional Differentiation between Synaptotagmins-1 and -7
Synaptotagmins are known to mediate diverse forms of Ca2+-triggered exocytosis through their C2 domains, but the principles underlying functional differentiation among them are unclear. Synaptotagmin-1 functions as a Ca2+ sensor in neurotransmitter release at central nervous system synapses, but synaptotagmin-7 does not, and yet both isoforms act as Ca2+ sensors in chromaffin cells. To shed light into this apparent paradox, we have performed rescue experiments in neurons from synaptotagmin-1 knockout mice using a chimera that contains the synaptotagmin-1 sequence with its C2B domain replaced by the synaptotagmin-7 C2B domain (Syt1/7). Rescue was not achieved either with the WT Syt1/7 chimera or with nine mutants where residues that are distinct in synaptotagmin-7 were restored to those present in synaptotagmin-1. To investigate whether these results arise because of unique conformational features of the synaptotagmin-7 C2B domain, we determined its crystal structure at 1.44 Ã… resolution. The synaptotagmin-7 C2B domain structure is very similar to that of the synaptotagmin-1 C2B domain and contains three Ca2+-binding sites. Two of the Ca2+-binding sites of the synaptotagmin-7 C2B domain are also present in the synaptotagmin-1 C2B domain and have analogous ligands to those determined for the latter by NMR spectroscopy, suggesting that a discrepancy observed in a crystal structure of the synaptotagmin-1 C2B domain arose from crystal contacts. Overall, our results suggest that functional differentiation in synaptotagmins arises in part from subtle sequence changes that yield dramatic functional differences