Author

A. Sottini

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:proteomics· 1 Approach:simulation· 1

Frequent Co-Authors

B. Schuler· 3 shared D. Nettels· 2 shared A. Borgia· 1 shared A. Chowdhury· 1 shared A. D. Due· 1 shared B. B. Kragelund· 1 shared B. Fierz· 1 shared C. B. Fernandes· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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3 shared papersBiophysics

B. Schuler

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Author profile →

3 papers

Recent·Most cited

The importance of stereochemistry in the disorder-order continuum of protein-protein interactions

E. A. Newcombe, A. D. Due, A. Sottini, C. B. Fernandes, L. Staby, E. Delaforge, C. R. O. Bartling, I. Brakti, K. Bugge, B. Schuler, K. Skriver, J. G. Olsen, B. B. Kragelund

The paper investigates the role of stereochemistry in disordered protein-protein interactions, finding that chirality is inconsequential in fully disordered complexes but essential when folding and binding are coupled.

bioRxiv · Feb 23, 2024 · PreprintBiophysics

Ultrafast molecular dynamics observed within a dense protein condensate

N. Galvanetto, M. T. Ivanovic, A. Chowdhury, A. Sottini, M. Nüesch, D. Nettels, R. Best, B. Schuler

The paper studies molecular dynamics in dense protein condensates, finding rapid sub-microsecond reconfiguration despite high viscosity.

bioRxiv · Dec 12, 2022Biophysics

Disordered Proteins Enable Histone Chaperoning on the Nucleosome

P. O. Heidarsson, D. Mercadante, A. Sottini, D. Nettels, M. B. Borgia, A. Borgia, S. Kilic, B. Fierz, R. B. Best, B. Schuler

The paper shows that disordered regions in proteins like H1 enable competitive displacement by histone chaperones such as prothymosin on the nucleosome.

bioRxiv · Apr 17, 2020Biophysics