Author

N. Chamachi

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 Assay:fluorescence / live-cell microscopy· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

A. Hartmann· 3 shared G. Krainer· 3 shared M. Schlierf· 3 shared A. Barth· 1 shared A. Kapanidis· 1 shared A. Sefer· 1 shared B. Ambrose· 1 shared C. A. M. Seidel· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiophysics

A. Hartmann

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3 papers

Recent·Most cited

Farewell to single-well: An automated single-molecule FRET platform for high-content, multiwell plate screening of biomolecular conformations and dynamics

A. Hartmann, K. Sreenivasa, M. Schenkel, N. Chamachi, P. Schake, G. Krainer, M. Schlierf

This paper introduces an automated multiwell plate platform for single-molecule FRET that enables high-content screening of biomolecular conformations and dynamics with improved accuracy and efficiency.

bioRxiv · Feb 28, 2023Biophysics

Reliability and accuracy of single-molecule FRET studies for characterization of structural dynamics and distances in proteins

G. Agam, C. Gebhardt, M. Popara, R. Maechtel, J. Folz, B. Ambrose, N. Chamachi, S. Y. Chung, T. D. Craggs, M. de Boer, D. Grohmann, T. Ha, A. Hartmann, J. Hendrix, V. Hirschfeld, , T. Cordes

This study evaluates the reliability and accuracy of single-molecule FRET for measuring protein structural dynamics and distances, finding high precision and accuracy with specific uncertainty limits.

bioRxiv · Aug 3, 2022Biophysics

Chaperones Skp and SurA dynamically expand unfolded outer membrane protein X and synergistically disassemble oligomeric aggregates

N. Chamachi, A. Hartmann, M. Q. Ma, G. Krainer, M. Schlierf

This study investigates how chaperones Skp and SurA interact with unfolded OmpX, showing they expand the protein and synergistically disassemble aggregates through dynamic and thermodynamic processes.

bioRxiv · Feb 23, 2021 · PreprintBiophysics