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1.
Phys Rev Lett ; 92(12): 125503, 2004 Mar 26.
Artigo em Inglês | MEDLINE | ID: mdl-15089684

RESUMO

We directly visualize single polymers with persistence lengths l(p), ranging from 0.05 to 16 microm, dissolved in the nematic phase of rodlike fd virus. Polymers with a sufficiently large persistence length undergo a coil-rod transition at the isotropic-nematic transition of the background solvent. We quantitatively analyze the transverse fluctuations of the semiflexible polymers and show that at long wavelengths they are driven by the fluctuating nematic background. We extract the Odijk deflection length and the elastic constant of the background nematic phase from the data.


Assuntos
Bacteriófago M13/química , Biopolímeros/química , Actinas/química , Bacteriófago lambda/genética , DNA Viral/química , Corantes Fluorescentes/química , Micelas , Proteínas de Neurofilamentos/química , Solventes
2.
Biophys J ; 79(6): 2987-3000, 2000 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-11106606

RESUMO

The red cell's spectrin-actin network is known to sustain local states of shear, dilation, and condensation, and yet the short actin filaments are found to maintain membrane-tangent and near-random azimuthal orientations. When calibrated with polarization results for single actin filaments, imaging of micropipette-deformed red cell ghosts has allowed an assessment of actin orientations and possible reorientations in the network. At the hemispherical cap of the aspirated projection, where the network can be dilated severalfold, filaments have the same membrane-tangent orientation as on a relatively unstrained portion of membrane. Likewise, over the length of the network projection pulled into the micropipette, where the network is strongly sheared in axial extension and circumferential contraction, actin maintains its tangent orientation and is only very weakly aligned with network extension. Similar results are found for the integral membrane protein Band 3. Allowing for thermal fluctuations, we deduce a bound for the effective coupling constant, alpha, between network shear and azimuthal orientation of the protofilament. The finding that alpha must be about an order of magnitude or more below its tight-coupling value illustrates how nanostructural kinematics can decouple from more macroscopic responses. Monte Carlo simulations of spectrin-actin networks at approximately 10-nm resolution further support this conclusion and substantiate an image of protofilaments as elements of a high-temperature spin glass.


Assuntos
Actinas/metabolismo , Citoesqueleto/ultraestrutura , Deformação Eritrocítica , Membrana Eritrocítica/fisiologia , Membrana Eritrocítica/ultraestrutura , Actinas/química , Animais , Proteína 1 de Troca de Ânion do Eritrócito/química , Proteína 1 de Troca de Ânion do Eritrócito/fisiologia , Calibragem , Simulação por Computador , Citoesqueleto/fisiologia , Microscopia de Fluorescência/métodos , Modelos Moleculares , Método de Monte Carlo , Músculo Esquelético/fisiologia , Conformação Proteica , Coelhos , Sensibilidade e Especificidade , Espectrina/química , Espectrina/metabolismo , Estresse Mecânico
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