Author

Valentin von Roten

University of ZurichORCID 0009-0002-9942-2854Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 3 Assay:fluorescence / live-cell microscopy· 2 Approach:deep learning· 1 Approach:experimental assay· 1 Approach:mechanistic / dynamical model· 1 Assay:proteomics· 1 Approach:simulation· 1 Assay:structural biology· 1

Frequent Co-Authors

Benjamin SchuleriD· 3 shared Miloš T. IvanovićiD· 3 shared Robert B. BestiD· 3 shared Andrea Holla· 2 shared Mark F. NüeschiD· 2 shared Andreas PresteliD· 1 shared Birthe Brandt KragelundiD· 1 shared Daniel NettelsiD· 1 shared

Activity by Year

2026-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiophysics

Benjamin SchulerORCID

Mutual co-authors in cluster

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3 papers

Recent·Most cited

BiophysicsbioRxivPreprintSep 15, 2026

Predictive all-atom simulations of disordered proteins and biomolecular condensates through osmometry-guided force-field optimization

Miloš T. Ivanović, Valentin von Roten, Benjamin Schuler, Robert B. Best

This paper optimizes force fields for simulating disordered proteins and condensates using osmometry data, improving agreement with experimental measurements.

DOI 10.64898/2026.08.25.747127

proteomicsdeep learning

𝕏 PostBluesky

BiophysicsbioRxivPreprintMay 24, 2026

Cooperativity, dynamics, and the free-energy surfaces of charge-patterned IDPs

Valentin von Roten, Miloš T. Ivanović, Soundhararajan Gopi…·Benjamin Schuler

This study examines how charge patterning affects the conformational behavior and dynamics of intrinsically disordered proteins using experimental techniques and simulations.

2 citations

fluorescence / live-cell microscopystructural biology

𝕏 PostBluesky

BiophysicsJACS AuPeer-reviewedMar 2, 2026

Dynamical buffering of reconfiguration dynamics in intrinsically disordered proteins

Miloš T. Ivanović, Andrea Holla, Mark F. Nüesch…·Robert B. Best

The paper investigates how sequence variation affects the dynamics of intrinsically disordered proteins, finding that reconfiguration times are largely independent of sequence despite changes in chain dimensions.

3 citationstop 4%

fluorescence / live-cell microscopysimulation

𝕏 PostBluesky