943 resultados para gelatin-SDS-PAGE


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page 10 pie

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data analysis table

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El presente trabajo de grado tiene como propósito evidenciar los cambios que se generaron en las dinámicas sociales de los residentes y comerciantes del barrio San Bernardo, cuando se decidió declarar este territorio idóneo para el Tratamiento de Renovación Urbana como resultado de una serie de especulaciones originadas por parte de la comunidad debido a la incertidumbre generada por la presencia de las entidades distritales en este barrio de Bogotá.

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Forma parte de una colección de libros de ficción estructurada en varias etapas, desde la diez a la catorce, y que tiene como finalidad que los alumnos de entre 7 y 11 años adquieran una mayor capacidad lectora. Para ello, las formas narrativas de las historias se hacen cada vez más complejas y se amplia el vocabulario de ellas; se aumentan el número de páginas y de texto y se reduce el número de ilustraciones. Sam y Lisa son reporteros del periódico de su clase, pero no saben sobre qué escribir. La desaparición de una cantidad de dinero motiva el interés de los dos amigos y les pone sobre la pista de un misterio que merece la primera página del periódico.

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Se plantea la problem??tica de los j??venes de la toma de decisiones, tales como elegir una carrera, una profesi??n, argument??ndose que en ocasiones no est??n preparados para tomar dicha decisi??n. Por ello se realiza un an??lisis de la obra Self-Directed Search, SDS, Forma Regular, Edici??n 1994 del profesor Holland, el cual trata de explicar la conducta vocacional de los j??venes. Se describen los fundamentos te??ricos expuestos en esta obra, las diferentes tipolog??as personales, tambi??n se aportan algunas cr??ticas que ha recibido esta obra, se detallan sus m??todos, sus instrumentos, su m??todo y sus resultados.

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Gelatin fibres have been successfully electrospun from water by heating a gelatin solution above the sol-gel transition temperature, and allowing cooling in a controlled environment as the fibres are produced. The development of structure with in these fibres is monitored using wide angle x-ray scattering, in this way the presence of the triple helix structure, which provides the physical cross-linkages in the gel could be probed. There is clear evidence that these structures are obtained in gelatin electrospun from aqueous solutions. In contrast fibres electrospun from a solution of gelatin in glacial acetic acid, showed no evidence of the triple helix structure.

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A scheme to describe SDS−lysozyme complex formation has been proposed on the basis of isothermal titration calorimetry (ITC) and FTIR spectroscopy data. ITC isotherms are convoluted and reveal a marked effect of both SDS and lysozyme concentration on the stoichiometry of the SDS−lysozyme complex. The binding isotherms have been described with the aid of FTIR spectroscopy in terms of changes in the lysozyme structure and the nature of the SDS binding. At low SDS concentrations, ITC isotherms feature an exothermic region that corresponds to specific electrostatic binding of SDS to positively charged amino acid residues on the lysozyme surface. This leads to charge neutralization of the complex and precipitation. The number of SDS molecules that bind specifically to lysozyme is approximately 8, as determined from our ITC isotherms, and is independent of lysozyme solution concentration. At high SDS concentrations, hydrophobic cooperative association dominates the binding process. Saturated binding stoichiometries as a molar ratio of SDS per molecule of lysozyme range from 220:1 to 80:1, depending on the lysozyme solution concentration. A limiting value of 78:1 has been calculated for lysozyme solution concentrations above 0.25 mM.

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Gel diagrams based on tube inversion and oscillatory rheometry are reported for Pluronic copolymers F127 (E98P67E98) and P123 (E21P67E21) in mixtures with anionic surfactant sodium dodecyl sulfate (SDS). Total concentrations (e, SDS+copolymer) were as high as 50 wt% with mole ratios SDS/copolymer (mr) in the ranges 1-5 (F127) a lid 1-7 (PI 23). Temperatures were its high as 90 degrees C. Determination of the temperature dependences of the dynamic moduli served to confirm the gel boundaries from tube inversion and to reveal the high elastic moduli of the gels, e.g., compared at corn parable positions in the gel phase, a 50 wt% SDS/P123 wit h mr = 7 had G' three times that of a corresponding gel of P123 alone. Sin all-angle X-ray scattering (SAX S) was used to show that the structures of all the SDS/F127 gels were bee and that the structures of the SDS/P123 gels with mr = I were either fcc(c = 30 wt%) or hex (c = 40 wt%). Assignment of structures to SDS/P123 gels with values of mr in the range 3-7 was more difficult, as high-order scattering peaks Could be very weak, and at the higher values of c and mr, the SAXS peaks included multiple reflections.

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A scheme to describe SDS-lysozyme complex formation has been proposed on the basis of isothermal titration calorimetry (ITC) and FTIR spectroscopy data. ITC isotherms are convoluted and reveal a marked effect of both SDS and lysozyme concentration on the stoichiometry of the SDS-lysozyme complex. The binding isotherms have been described with the aid of FTIR spectroscopy in terms of changes in the lysozyme structure and the nature of the SDS binding. At low SDS concentrations, ITC isotherms feature an exothermic region that corresponds to specific electrostatic binding of SDS to positively charged amino acid residues on the lysozyme surface. This leads to charge neutralization of the complex and precipitation. The number of SDS molecules that bind specifically to lysozyme is approximately 8, as determined from our ITC isotherms, and is independent of lysozyme solution concentration. At high SDS concentrations, hydrophobic cooperative association dominates the binding process. Saturated binding stoichiometries as a molar ratio of SDS per molecule of lysozyme range from 220: 1 to 80: 1, depending on the lysozyme solution concentration. A limiting value of 78: 1 has been calculated for lysozyme solution concentrations above 0.25 mM.

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