Author

F. E. Thomasen

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

Biology Disciplines

Click to filter author papers

Biophysics· 4

Signature Assays, Organisms & Methods

Click to filter · or open tag

Research Focus:protein folding & dynamics· 3 Approach:experimental assay· 2 Approach:statistical model· 2 Approach:mechanistic / dynamical model· 1 Assay:protein structure· 1 Assay:structural biology· 1

Frequent Co-Authors

K. Lindorff-Larsen· 4 shared M. J. Cuneo· 2 shared T. Mittag· 2 shared A. Kumar· 1 shared A. Nourse· 1 shared C. R. Grace· 1 shared E. W. Martin· 1 shared F. Pesce· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

4 shared papersBiophysics

K. Lindorff-Larsen

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Rescaling protein-protein interactions improves Martini 3 for flexible proteins in solution

F. E. Thomasen, T. Skaalum, A. Kumar, S. Srinivasan, S. Vanni, K. Lindorff-Larsen

This study improves the Martini 3 model by reducing protein-protein interaction strength, enhancing accuracy for flexible proteins in solution and with lipid membranes.

bioRxiv · May 29, 2023 · PreprintBiophysics

Conformational and oligomeric states of SPOP from small-angle X-ray scattering and molecular dynamics simulations

F. E. Thomasen, M. J. Cuneo, T. Mittag, K. Lindorff-Larsen

This study characterizes SPOP's conformational and oligomeric states using SAXS and molecular dynamics simulations, revealing rigid helical structures with flexible linker regions.

bioRxiv · Oct 8, 2022Biophysics

Improving Martini 3 for disordered and multidomain proteins

F. E. Thomasen, F. Pesce, M. A. Roesgaard, G. Tesei, K. Lindorff-Larsen

This study improves the Martini 3 force field for simulating disordered and multidomain proteins by adjusting protein-water interactions to better match experimental data.

bioRxiv · Oct 1, 2021Biophysics

Interplay of folded domains and the disordered low-complexity domain in mediating hnRNPA1 phase separation

E. W. Martin, F. E. Thomasen, N. M. Milkovic, M. J. Cuneo, C. R. Grace, A. Nourse, K. Lindorff-Larsen, T. Mittag

This study investigates how folded domains of hnRNPA1 modulate phase separation behavior of its disordered low-complexity domain, showing salt-dependent effects through electrostatic interactions and solubility changes.

bioRxiv · May 15, 2020Biophysics