Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 9 de 9
Filtrar
1.
Opt Lett ; 40(6): 906-9, 2015 Mar 15.
Artículo en Inglés | MEDLINE | ID: mdl-25768143

RESUMEN

We demonstrate the optical levitation or trapping in helium gas of a single quantum dot (QD) within a liquid droplet. Bright single photon emission from the levitated QD in the droplet was observed for more than 200 s. The observed photon count rates are consistent with the value theoretically estimated from the two-photon-action cross section. This Letter presents the realization of an optically levitated solid-state quantum emitter.


Asunto(s)
Pinzas Ópticas , Puntos Cuánticos , Rayos Láser , Dispersión de Radiación
2.
Phys Rev Lett ; 108(16): 160601, 2012 Apr 20.
Artículo en Inglés | MEDLINE | ID: mdl-22680705

RESUMEN

When a Brownian object interacts with noninteracting gas particles under nonequilibrium conditions, energy dissipation associated with Brownian motion causes an additional force on the object as a "momentum transfer deficit." This principle is demonstrated first by a new nonequilibrium steady state model and then applied to several known models such as an adiabatic piston for which a simple explanation has been lacking.

3.
Mol Biol Cell ; 32(5): 446-459, 2021 03 01.
Artículo en Inglés | MEDLINE | ID: mdl-33405949

RESUMEN

The components and subprocesses underlying the formation of COPI-coated vesicles at the Golgi are well understood. The coating cascade is initiated after the small GTPase Arf1 is activated by the Sec7 domain-containing guanine nucleotide exchange factor GBF1 (Golgi brefeldin A resistant guanine nucleotide exchange factor 1). This causes a conformational shift within Arf1 that facilitates stable association of Arf1 with the membrane, a process required for subsequent recruitment of the COPI coat. Although we have atomic-level knowledge of Arf1 activation by Sec7 domain-containing GEFs, our understanding of the biophysical processes regulating Arf1 and GBF1 dynamics is limited. We used fluorescence recovery after photobleaching data and kinetic Monte Carlo simulation to assess the behavior of Arf1 and GBF1 during COPI vesicle formation in live cells. Our analyses suggest that Arf1 and GBF1 associate with Golgi membranes independently, with an excess of GBF1 relative to Arf1. Furthermore, the GBF1-mediated Arf1 activation is much faster than GBF1 cycling on/off the membrane, suggesting that GBF1 is regulated by processes other than its interactions Arf1. Interestingly, modeling the behavior of the catalytically inactive GBF1/E794K mutant stabilized on the membrane is inconsistent with the formation of a stable complex between it and an endogenous Arf1 and suggests that GBF1/E794K is stabilized on the membrane independently of complex formation.


Asunto(s)
Factor 1 de Ribosilacion-ADP/metabolismo , Vesículas Cubiertas por Proteínas de Revestimiento/metabolismo , Factores de Intercambio de Guanina Nucleótido/metabolismo , Factor 1 de Ribosilacion-ADP/fisiología , Factores de Ribosilacion-ADP/metabolismo , Vesículas Cubiertas por Proteínas de Revestimiento/fisiología , Proteína Coat de Complejo I/metabolismo , Endocitosis , Retículo Endoplásmico/metabolismo , Recuperación de Fluorescencia tras Fotoblanqueo/métodos , Aparato de Golgi/metabolismo , Factores de Intercambio de Guanina Nucleótido/fisiología , Células HeLa , Humanos , Cinética , Proteínas de Unión al GTP Monoméricas/metabolismo , Método de Montecarlo , Unión Proteica , Transporte de Proteínas
4.
Phys Rev Lett ; 105(15): 150603, 2010 Oct 08.
Artículo en Inglés | MEDLINE | ID: mdl-21230882

RESUMEN

We study the efficiency at maximum power, η*, of engines performing finite-time Carnot cycles between a hot and a cold reservoir at temperatures Th and Tc, respectively. For engines reaching Carnot efficiency ηC=1-Tc/Th in the reversible limit (long cycle time, zero dissipation), we find in the limit of low dissipation that η* is bounded from above by ηC/(2-ηC) and from below by ηC/2. These bounds are reached when the ratio of the dissipation during the cold and hot isothermal phases tend, respectively, to zero or infinity. For symmetric dissipation (ratio one) the Curzon-Ahlborn efficiency ηCA=1-√Tc/Th] is recovered.

5.
Mol Biol Cell ; 17(7): 2996-3008, 2006 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-16624868

RESUMEN

The mechanisms regulating membrane recruitment of the p115 tethering factor in vivo are unknown. Here, we describe cycling of p115 between membranes and cytosol and document the effects of Golgi matrix proteins, Rab1, and soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs) on this process. Rapid membrane/cytosol exchange is shown by swift (t1/2 approximately 20 s) loss of Golgi-localized p115-green fluorescent protein (GFP) after repeated photobleaching of cell periphery and rapid (t1/2 approximately 13 s) fluorescence recovery after photobleaching Golgi-localized p115-GFP. p115 mutant missing the GM130/giantin binding site exhibits analogous fluorescence recovery after photobleaching (FRAP) (t1/2 approximately 13 s), suggesting that GM130 and giantin are not major determinants of p115 membrane dynamics. In contrast, p115-GFP exchanges more rapidly (t1/2 approximately 8 s) in cells expressing the inactive Rab1/N121I mutant, indicating that p115 cycling is influenced by Rab1. p115-GFP dynamics is also influenced by the assembly status of SNAREs. In cells expressing an ATPase-deficient NSF/E329Q mutant that inhibits SNARE complex disassembly, the cycling kinetics of p115-GFP are significantly slower (t1/2 approximately 21 s). In contrast, in cells incubated at reduced temperature (10 degrees C) that inhibits vesicular traffic, the cycling kinetics of p115-GFP are faster (t1/2 approximately 7 s). These data suggest that p115-binding sites on the membrane are provided by unassembled SNAREs. In agreement, biochemical studies show increased p115 recruitment to membranes in the presence of NSF and alpha-SNAP. Our data support a model in which recruitment of tethers is directly regulated by the assembly status of SNAREs.


Asunto(s)
Retículo Endoplásmico/metabolismo , Aparato de Golgi/metabolismo , Membranas Intracelulares/metabolismo , Proteínas de la Membrana/metabolismo , Proteínas SNARE/metabolismo , Proteínas de Transporte Vesicular/metabolismo , Animales , Autoantígenos , Citosol/química , Citosol/metabolismo , Retículo Endoplásmico/química , Proteínas de la Matriz de Golgi , Proteínas Fluorescentes Verdes/análisis , Proteínas Fluorescentes Verdes/genética , Humanos , Membranas Intracelulares/química , Cinética , Proteínas de la Membrana/análisis , Proteínas de la Membrana/genética , Proteínas Sensibles a N-Etilmaleimida/metabolismo , Transporte de Proteínas , Ratas , Proteínas de Transporte Vesicular/análisis , Proteínas de Transporte Vesicular/genética , Proteínas de Unión al GTP rab1/genética , Proteínas de Unión al GTP rab1/metabolismo
6.
Phys Rev E Stat Nonlin Soft Matter Phys ; 77(5 Pt 1): 051132, 2008 May.
Artículo en Inglés | MEDLINE | ID: mdl-18643051

RESUMEN

We investigate the energetics of a Brownian motor driven by position-dependent temperature, commonly known as the Büttiker-Landauer motor. Overdamped models (M=0) predict that the motor can attain Carnot efficiency. However, the overdamped limit (M-->0) contradicts the previous prediction due to the kinetic energy contribution to the heat transfer. Using molecular dynamics simulation and numerical solution of the inertial Langevin equation, we confirm that the motor can never achieve Carnot efficiency and verify that the heat flow via kinetic energy diverges as M{-1/2} in the overdamped limit. The reciprocal process of the motor, namely, the Büttiker-Landauer refrigerator, is also examined. In this case, the overdamped approach succeeds in predicting the heat transfer only when there is no temperature gradient. Its found that the Onsager symmetry between the motor and refrigerator does not suffer from the singular behavior of the kinetic energy contribution.

7.
Phys Rev E Stat Nonlin Soft Matter Phys ; 74(1 Pt 1): 011912, 2006 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-16907132

RESUMEN

We investigated three models of Brownian motors which convert rotational diffusion into directed translational motion by switching on and off a potential. In the first model a spatially asymmetric potential generates directed translational motion by rectifying rotational diffusion. It behaves much like a conventional flashing ratchet. The second model utilizes both rotational diffusion and drift to generate translational motion without spatial asymmetry in the potential. This second model can be driven by a combination of a Brownian motor mechanism (diffusion driven) or by powerstroke (drift driven) depending on the chosen parameters. In the third model, elements of both the Brownian motor and powerstroke mechanisms are combined by switching between three distinct states. Relevance of the model to biological motor proteins is discussed.


Asunto(s)
Transferencia de Energía , Modelos Químicos , Modelos Moleculares , Proteínas Motoras Moleculares/química , Simulación por Computador , Difusión , Movimiento (Física) , Rotación , Estrés Mecánico
8.
J Mol Biol ; 322(5): 1065-88, 2002 Oct 04.
Artículo en Inglés | MEDLINE | ID: mdl-12367529

RESUMEN

We have formulated a three-compartment model of muscle activation that includes both strong cross-bridge (XB) and Ca(2+)-activated regulatory-unit (RU) mediated nearest-neighbor cooperative influences. The model is based on the tight coupling premise--that XB retain activating Ca(2+) on the thin filament. Using global non-linear least-squares, the model produced excellent fits to experimental steady-state force-pCa and ATPase-pCa data from skinned rat soleus fibers. In terms of the model, nearest-neighbor influences over the range of Ca(2+) required for activation cause the Ca(2+) dissociation rate from regulatory-units (k(off)) to decrease and the cross-bridge association rate (f) to increase each more than ten-fold. Moreover, the rate variations occur in separate Ca(2+) regimes. The energy of activation governing f is strongly influenced by both neighboring RU and XB. In contrast, the energy of activation governing k(off) is less affected by neighboring XB than by neighboring RU. Nearest-neighbor cooperative influences provide both an overall sensitization to Ca(2+) and the well-known steep response of force to free Ca(2+). The apparent sensitivity for Ca(2+)-activation of force and ATPase is a function of cross-bridge kinetic rates. The model and derived parameter set produce simulated behavior in qualitative agreement with steady-state experiments reported in the literature for partial TnC replacement, increased [P(i)], increased [ADP], and MalNEt-S1 addition. The model is an initial attempt to construct a general theory of striated muscle activation-one that can be consistently used to interpret data from various types of muscle manipulation experiments.


Asunto(s)
Citoesqueleto de Actina/metabolismo , Modelos Biológicos , Contracción Muscular/fisiología , Músculo Esquelético/metabolismo , Adenosina Difosfato/metabolismo , Adenosina Trifosfatasas/metabolismo , Animales , Calcio/metabolismo , Inhibidores Enzimáticos/farmacología , Etilmaleimida/farmacología , Matemática , Músculo Esquelético/citología , Músculo Esquelético/efectos de los fármacos , Fosfatos/metabolismo , Ratas , Troponina C/metabolismo
9.
Phys Rev E Stat Nonlin Soft Matter Phys ; 81(4 Pt 1): 041106, 2010 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-20481676

RESUMEN

We evaluate the efficiency at maximum power of a quantum-dot Carnot heat engine. The universal values of the coefficients at the linear and quadratic order in the temperature gradient are reproduced. Curzon-Ahlborn efficiency is recovered in the limit of weak dissipation.


Asunto(s)
Calor , Puntos Cuánticos , Frío , Modelos Teóricos
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA