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Boeri Erba

As seen in: Nature, Frontiers
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Articles

Hierarchical folding-upon-binding of an intrinsically disordered protein

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By Mariño Pérez, Boeri Erba, Luiza Mamigonian
| docusalut.com
Intrinsically disordered proteins (IDPs) often undergo folding-upon-binding to their partners via short linear motifs, typically 5-15 amino acids in length. However, a significant proportion of IDPs do not adhere to this paradigm but fold upon binding through extended regions comprising multiple molecular recognition elements. For these IDPs, the binding mechanisms and the structural characteristics of their folding intermediates remain poorly understood.
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Sequencing intact membrane proteins using MALDI mass spectrometry

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By Boeri Erba, Martin d'Hères, Zhamungui Sánchez
| Frontiers
Sequencing intact membrane proteins using MALDI mass spectrometry 1Commissariat à l'Energie Atomique et aux Energies Alternatives (CEA), France 2UMR5075 Institut de Biologie Structurale (IBS), France 3Université Grenoble Alpes, France 4UPR4301 Centre de biophysique moléculaire (CBM), France 5University of Turin, Italy The final, formatted version of the article will be published soon.
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PDB-wide identification of biological assemblies from conserved quaternary structure geometry

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By R. L. Jr., Boeri Erba, David Ritchie, Sucharita Dey
| Nature Verified
Protein structures are key to understanding biomolecular mechanisms and diseases, yet their interpretation is hampered by limited knowledge of their biologically relevant quaternary structure (QS). A critical challenge in inferring QS information from crystallographic data is distinguishing biological interfaces from fortuitous crystal-packing contacts. Here, we tackled this problem by developing strategies for aligning and comparing QS states across both homologs and data repositories.
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