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Maddalena BinDoktorand

Om mig

I am a Ph.D. student in the Structural dynamics of aqueous solutions (SDAQS) group and my research interest is on protein structural dynamics and how the anomalous properties of water affect the structure and dynamics of biomolecules.

In my project, I conduct experiments on hydrated and cryoprotected proteins from room temperature down to cryogenic conditions employing X-ray scattering techniques, such as Small- and Wide-Angle X-ray Scattering (SAXS and WAXS) and X-ray Photon Correlation Spectroscopy (XPCS).

I first joined the SDAQS group for my master thesis project with the Erasmus+ program. After graduating from the University of Padova (Italy) I started doctoral studies here under the supervision of Prof. F. Perakis.

Forskningsprojekt

Hur beter sig biomolekyler i cellens trånga miljö?

Insidan av en cell är fullpackad med proteiner, RNA och andra biomolekyler. Forskare har upptäckt att denna trängsel i cellen resulterar i ett slags kondensat av biomolekyler, som små molekyldroppar, som verkar vara viktiga för cellens funktion.

Biomolekyler i trånga miljöer

Publikationer

I urval från Stockholms universitets publikationsdatabas

  • Wide-angle X-ray scattering and molecular dynamics simulations of supercooled protein hydration water

    2021. Maddalena Bin (et al.). Physical Chemistry, Chemical Physics - PCCP 23 (34), 18308-18313

    Artikel

    Understanding the mechanism responsible for the protein low-temperature crossover observed at T approximate to 220 K can help us improve current cryopreservation technologies. This crossover is associated with changes in the dynamics of the system, such as in the mean-squared displacement, whereas experimental evidence of structural changes is sparse. Here we investigate hydrated lysozyme proteins by using a combination of wide-angle X-ray scattering and molecular dynamics (MD) simulations. Experimentally we suppress crystallization by accurate control of the protein hydration level, which allows access to temperatures down to T = 175 K. The experimental data indicate that the scattering intensity peak at Q = 1.54 angstrom(-1), attributed to interatomic distances, exhibits temperature-dependent changes upon cooling. In the MD simulations it is possible to decompose the water and protein contributions and we observe that, while the protein component is nearly temperature independent, the hydration water peak shifts in a fashion similar to that of bulk water. The observed trends are analysed by using the water-water and water-protein radial distribution functions, which indicate changes in the local probability density of hydration water.

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