Materials Map

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The Materials Map is an open tool for improving networking and interdisciplinary exchange within materials research. It enables cross-database search for cooperation and network partners and discovering of the research landscape.

The dashboard provides detailed information about the selected scientist, e.g. publications. The dashboard can be filtered and shows the relationship to co-authors in different diagrams. In addition, a link is provided to find contact information.

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The Materials Map is still under development. In its current state, it is only based on one single data source and, thus, incomplete and contains duplicates. We are working on incorporating new open data sources like ORCID to improve the quality and the timeliness of our data. We will update Materials Map as soon as possible and kindly ask for your patience.

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in Cooperation with on an Cooperation-Score of 37%

Topics

Publications (2/2 displayed)

  • 2021Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR125citations
  • 2021Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR111citations

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Palomino-Schätzlein, Martina
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Iovanna, Juan L.
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Pierattelli, Roberta
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Molina, Paula Malo De
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Neira, José L.
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Bonucci, Alessio
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Malo De Molina, Paula
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Arbe Méndez, María Aranzazu
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2021

Co-Authors (by relevance)

  • Palomino-Schätzlein, Martina
  • Iovanna, Juan L.
  • Pierattelli, Roberta
  • Molina, Paula Malo De
  • Neira, José L.
  • Bonucci, Alessio
  • Arbe, Arantxa
  • Malo De Molina, Paula
  • Arbe Méndez, María Aranzazu
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article

Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1

  • Palomino-Schätzlein, Martina
  • Rizzuti, Bruno
  • Iovanna, Juan L.
  • Pierattelli, Roberta
  • Molina, Paula Malo De
  • Neira, José L.
  • Bonucci, Alessio
  • Arbe, Arantxa
Abstract

<jats:p>The intracellular environment is crowded with macromolecules, including sugars, proteins and nucleic acids. In the cytoplasm, crowding effects are capable of excluding up to 40% of the volume available to any macromolecule when compared to dilute conditions. NUPR1 is an intrinsically disordered protein (IDP) involved in cell-cycle regulation, stress-cell response, apoptosis processes, DNA binding and repair, chromatin remodeling and transcription. Simulations of molecular crowding predict that IDPs can adopt compact states, as well as more extended conformations under crowding conditions. In this work, we analyzed the conformation and dynamics of NUPR1 in the presence of two synthetic polymers, Ficoll-70 and Dextran-40, which mimic crowding effects in the cells, at two different concentrations (50 and 150 mg/ml). The study was carried out by using a multi-spectroscopic approach, including: site-directed spin labelling electron paramagnetic resonance spectroscopy (SDSL-EPR), nuclear magnetic resonance spectroscopy (NMR), circular dichroism (CD), small angle X-ray scattering (SAXS) and dynamic light scattering (DLS). SDSL-EPR spectra of two spin-labelled mutants indicate that there was binding with the crowders and that the local dynamics of the C and N termini of NUPR1 were partially affected by the crowders. However, the overall disordered nature of NUPR1 did not change substantially in the presence of the crowders, as shown by circular dichroism CD and NMR, and further confirmed by EPR. The changes in the dynamics of the paramagnetic probes appear to be related to preferred local conformations and thus crowding agents partially affect some specific regions, further pinpointing that NUPR1 flexibility has a key physiological role in its activity.</jats:p>

Topics
  • impedance spectroscopy
  • polymer
  • simulation
  • electron spin resonance spectroscopy
  • Nuclear Magnetic Resonance spectroscopy
  • small angle x-ray scattering
  • dynamic light scattering