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1.
Microscopy (Oxf) ; 2024 Apr 25.
Artigo em Inglês | MEDLINE | ID: mdl-38661285

RESUMO

We report that the spin vector of photoelectrons emitted from an atomic layer Pb grown on a germanium substrate [Pb/Ge(111)] can be controlled using an electric field of light. The spin polarization of photoelectrons excited by a linearly polarized light is precisely investigated by spin- and angle-resolved photoemission spectroscopy. The spin polarization of the photoelectrons observed in the mirror plane reverses between p- and s-polarized lights. Considering the dipole transition selection rule, the surface state of Pb/Ge(111) is represented by a linear combination of symmetric and asymmetric orbital components coupled with spins in mutually opposite directions. The spin direction of the photoelectrons is different from that of the initial state when the electric field vector of linearly polarized light deviates from p- or s-polarization conditions. The quantum interference in the photoexcitation process can determine the direction of the spin vector of photoelectrons.

2.
J Theor Biol ; 281(1): 65-73, 2011 Jul 21.
Artigo em Inglês | MEDLINE | ID: mdl-21514305

RESUMO

Actomyosin contractility is a major force-generating mechanism that drives rearrangement of actomyosin networks; it is fundamental to cellular functions such as cellular reshaping and movement. Thus, to clarify the mechanochemical foundation of the emergence of cellular functions, understanding the relationship between actomyosin contractility and rearrangement of actomyosin networks is crucial. For this purpose, in this study, we present a new particulate-based model for simulating the motions of actin, non-muscle myosin II, and α-actinin. To confirm the model's validity, we successfully simulated sliding and bending motions of actomyosin filaments, which are observed as fundamental behaviors in dynamic rearrangement of actomyosin networks in migrating keratocytes. Next, we simulated the dynamic rearrangement of actomyosin networks. Our simulation results indicate that an increase in the density fraction of myosin induces a higher-order structural transition of actomyosin filaments from networks to bundles, in addition to increasing the force generated by actomyosin filaments in the network. We compare our simulation results with experimental results and confirm that actomyosin bundles bridging focal adhesions and the characteristics of myosin-dependent rearrangement of actomyosin networks agree qualitatively with those observed experimentally.


Assuntos
Actomiosina/metabolismo , Modelos Biológicos , Miosinas/metabolismo , Citoesqueleto de Actina/metabolismo , Actinina/metabolismo , Fenômenos Biomecânicos/fisiologia , Simulação por Computador , Reagentes de Ligações Cruzadas/metabolismo , Contração Muscular/fisiologia
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