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223 results on '"Fermani S."'

10. Ecomorphological, behavioural and physiological patterns in otoliths

Author

Palazzo Q., Stagioni M., Raaijmakers S., Belleman R. G., Prada F., Fermani S., Hammel J. U., Kaandorp J., Goffredo S., Falini G., and Palazzo Q., Stagioni M., Raaijmakers S., Belleman R.G., Prada F., Fermani S., Hammel J.U., Kaandorp J., Goffredo S., Falini G.

Subjects
otoliths
Published
2021

38. Polypeptide effect on Mg2+ hydration inferred from CaCO3 formation: A biomineralization study by counter-diffusion

Author

Sancho Tomás, María, Fermani, S., Reggi, M., García Ruiz, Juan Manuel, Gómez-Morales, Jaime, Falini, G., Sancho Tomás, María, Fermani, S., Reggi, M., García Ruiz, Juan Manuel, Gómez-Morales, Jaime, and Falini, G.

Abstract

The use of a counter-diffusion system allows the evaluation of diverse parameters involved in a crystallization process. In this study, this tool has been used to infer the hydration status of Mg during CaCO formation experiments in an agarose highly viscous sol entrapping charged polypeptides. The experimental data allow us to infer that the hydration status of Mg is altered by the presence of poly-l-aspartate or poly-l-glutamate. This changes the CaCO polymorphic distribution in favor of Mg-calcite with respect to aragonite, but does not favor the isomorphic substitution of Mg with Ca within the calcite lattice. The latter may exclude the formation of an amorphous transient form, which leads to a high Mg-calcite, as expected when using a counter-diffusion system set up. The presence of poly-l-lysine does not affect the hydration of Mg, but favors the formation of aragonite with respect to calcite. In this case an inhibition of calcite formation and an alteration of the hydration sphere of Ca could be invoked; both effects are able to increase CaCO supersaturation. In conclusion, this study reveals that charged polypeptides can orchestrate CaCO formation by also controlling the hydration status of cations.

Published
2016

42. Identificación y análisis físico y social de eventos destructivos de origen geológico e hidrológico: resultados finales del proyecto

Author

Cisneros, Héctor, Carini, F., Fermani, S., Ahumada, María Nélida, and Torres, Jorge

Subjects
geológico e hidrológico, eventos destructivos
Abstract

Fil: Cisneros, Héctor. Universidad Juan Agustín Maza; Universidad Nacional de Cuyo; Universidad Nacional de San Luis. República Argentina Fil: Carini, F. Universidad Nacional de San Luis. República Argentina Fil: Fermani, S. Universidad de Congreso. Mendoza. República Argentina. Fil: Ahumada, María Nélida. Universidad Juan Agustín Maza. Mendoza. República Argentina Fil: Torres, Jorge. Universidad Tecnológica Argentina Regional Mendoza. Maestría en Desarrollo Sustentable del hábitat Humano. Mendoza. República Argentina La comarca ubicada en el sector centro-norte de la provincia de Mendoza, conocida como “Gran Mendoza”, con una población aproximada de 1.000.000 de habitantes, es considerada como una de las regiones del país con mayor vulnerabilidad ante eventos destructivos de origen geológico e hidrológico. Respecto al primero, en la zona pedemontana de Mendoza y San juan se concentran más del 80% de las estructuras sismogénicas activas del sector continental argentino. Por otro lado, los aluviones han demostrado ser el fenómeno catastrófico que más daños ha causado a la región metropolitana de esta provincia. Por estas razones se hace evidente la necesidad de estudiar las características de estos eventos, el peligro sísmico y aluvional, y de realizar efectivas evaluaciones de riesgo. La metodología usada incluye la sistematización de los datos y su presentación cartográfica con geotecnologías SIG y de Teledetección. Se presentan en esta contribución los resultados del estudio realizado en el marco del proyecto acreditado por la Universidad Juan Agustín Maza.

Published
2014

44. Biochemical basis of sulphenomics: how protein sulphenic acids may be stabilized by the protein microenvironment.

Author

Trost, P., Fermani, S., Calvaresi, M., and Zaffagnini, M.

Subjects
*SULFENIC acids, *CYSTEINE, *POST-translational modification, *REACTIVE oxygen species, *REACTIVE nitrogen species
Abstract

Among protein residues, cysteines are one of the prominent candidates to ROS-mediated and RNS-mediated post-translational modifications, and hydrogen peroxide (H2O2) is the main ROS candidate for inducing cysteine oxidation. The reaction with H2O2 is not common to all cysteine residues, being their reactivity an utmost prerequisite for the sensitivity towards H2O2. Indeed, only deprotonated Cys (i.e. thiolate form, S−) can react with H2O2 leading to sulphenic acid formation (SOH), which is considered as a major/central player of ROS sensing pathways. However, cysteine sulphenic acids are generally unstable because they can be further oxidized to irreversible forms (sulphinic and sulphonic acids, SO2H and SO3H, respectively), or alternatively, they can proceed towards further modifications including disulphide bond formation (SS), S-glutathionylation (SSG) and sulphenamide formation (SN). To understand why and how cysteine residues undergo primary oxidation to sulphenic acid, and to explore the stability of cysteine sulphenic acids, a combination of biochemical, structural and computational studies are required. Here, we will discuss the current knowledge of the structural determinants for cysteine reactivity and sulphenic acid stability within protein microenvironments. [ABSTRACT FROM AUTHOR]

Published
2017
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49. Crystallization of proteins on functionalized surfaces.

Author

Tosi, G., Fermani, S., Falini, G., Gavira Gallardo, J. A., García Ruiz, Juan Manuel, Tosi, G., Fermani, S., Falini, G., Gavira Gallardo, J. A., and García Ruiz, Juan Manuel

Abstract

Functionalized mica sheets and polystyrene films exposing ionisable groups have been used as heterogeneous nucleating surfaces for model proteins. Surfaces with different densities of amino or sulfonated groups have been prepared. Crystallization trials were carried out using the hanging-drop vapour-diffusion method. The results show that using these surfaces the starting protein concentration necessary to form crystals is reduced. The effect of these surfaces on the crystallization process may be the consequence of electrostatic interactions between charged residues of proteins and ionisable groups on surfaces. These interactions can be attractive or repulsive, depending on the relative charge of the protein and the surface at the crystallization pH. Both phenomena can induce an increase of the local protein concentration on the surface or in its proximity, favouring nucleation. Moreover, a reduction of the waiting time (an estimation of the nucleation time) was also observed for some proteins, suggesting a surface-stabilization effect on crystal nuclei.

Published
2008

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