Author

K. Schweimer

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 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Approach:biophysical modeling· 2 Research Focus:cell type annotation· 2 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:protein folding & dynamics· 2 Assay:protein sequence· 2 Assay:protein structure· 2 Approach:statistical model· 2

Frequent Co-Authors

P. K. Zuber· 2 shared S. H. Knauer· 2 shared A. A. Jalan· 1 shared A. Lomoschitz· 1 shared B. Höcker· 1 shared B. Simon· 1 shared C. Hayn· 1 shared F. Gebauer· 1 shared

Activity by Year

2018-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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2 shared papersBiophysics

P. K. Zuber

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Author profile →

4 papers

Recent·Most cited

The Drosophila RNA binding protein Hrp48 binds a specificRNA sequence of the msl-2 mRNA 3' UTR to regulatetranslation

A. Lomoschitz, J. Meyer, T. Guitart, M. Krepl, K. Lapouge, C. Hayn, K. Schweimer, B. Simon, J. Sponer, F. Gebauer, J. Hennig

This paper identifies the RNA binding specificity of Hrp48, showing it binds the msl-2 mRNA 3' UTR independently of Sxl and Unr downstream of their binding sites.

bioRxiv · Mar 26, 2024 · PreprintBiophysics

Hydrophobic Clusters Direct Folding of a Synthetic Chimeric Protein

A. A. Jalan, L. Hassine, S. Romero-Romero, J. Hübner, K. Schweimer, B. Höcker

This study investigates how hydrophobic clusters influence the folding and stability of a synthetic chimeric protein made from fragments of two different proteins.

bioRxiv · Sep 29, 2023 · PreprintBiophysics

Structural and thermodynamic analyses of the β-to-α transformation in RfaH reveal principles of fold-switching proteins

P. K. Zuber, T. Daviter, R. Heissmann, U. Persau, K. Schweimer, S. H. Knauer

This study analyzes the structural and thermodynamic properties of RfaH and NusG/Spt5-KOW domains to understand the mechanisms of fold-switching in proteins.

bioRxiv · Jan 14, 2022Biophysics

The universally-conserved transcription factor RfaH is recruited to a hairpin structure of the non-template DNA strand

P. K. Zuber, I. Artsimovitch, M. NandyMazumdar, Z. Liu, Y. Nedialkov, K. Schweimer, P. Roesch, S. H. Knauer

The paper shows RfaH, a transcription factor, binds to a hairpin structure in the non-template DNA strand via a conserved pause sequence, revealing a new mechanism for transcriptional regulation.

bioRxiv · Apr 26, 2018Biochemistry