Author

Miloš T. Ivanović

University of ZurichORCID 0000-0003-3164-9411Unclaimed 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 Approach:experimental assay· 2 Assay:fluorescence / live-cell microscopy· 2 Approach:deep learning· 1 Organism:Drosophila· 1 Approach:mechanistic / dynamical model· 1 Assay:proteomics· 1 Approach:simulation· 1

Frequent Co-Authors

Benjamin SchuleriD· 3 shared Robert B. BestiD· 3 shared Valentin von RoteniD· 3 shared Andrea Holla· 2 shared Mark F. NüeschiD· 2 shared Andreas PresteliD· 1 shared Bernd SimoniD· 1 shared Birthe Brandt KragelundiD· 1 shared

Activity by Year

2021-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiophysics

Benjamin SchulerORCID

Mutual co-authors in cluster

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4 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

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Molecular BiologyNucleic Acids ResearchPeer-reviewedJul 27, 2021

Structure and dynamics of the quaternary hunchback mRNA translation repression complex

Jakub Macošek, Bernd Simon, Johanna-Barbara Linse…·Janosch Hennig

The paper characterizes the quaternary hunchback mRNA repression complex formed by Brat, Pum, and Nanos, revealing its flexibility and independent binding of RNA components.

11 citations

Drosophilaexperimental assay

𝕏 PostBluesky