Author

E. E. Tranchant

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· 2 Research Focus:cell type annotation· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1 Organism:yeast· 1

Frequent Co-Authors

B. B. Kragelund· 3 shared F. Pesce· 3 shared K. Lindorff-Larsen· 3 shared E. A. Newcombe· 2 shared N. L. Jacobsen· 2 shared A. Prestel· 1 shared C. B. Fernandes· 1 shared C. R. Grace· 1 shared

Activity by Year

2022-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 34 mutual co-author links

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3 shared papersBiophysics

B. B. Kragelund

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3 papers

Recent·Most cited

Revisiting the use of dioxane as a reference compound for determination of the hydrodynamic radius of proteins by pulsed field gradient NMR spectroscopy

E. E. Tranchant, F. Pesce, N. L. Jacobsen, C. B. Fernandes, B. B. Kragelund, K. Lindorff-Larsen

The paper revisits the use of dioxane as a reference compound in PFG NMR to determine protein hydrodynamic radius, finding the current reference value underestimated and proposing a new value.

bioRxiv · Jun 2, 2023 · PreprintBiophysics

Deciphering the alphabet of disorder -- Glu and Asp act differently on local but not global properties

M. A. Roesgaard, J. E. Lundsgaard, E. A. Newcombe, N. L. Jacobsen, F. Pesce, E. E. Tranchant, S. Lindemose, A. Prestel, R. Hartmann-Petersen, K. Lindorff-Larsen, B. B. Kragelund

This study compares the functional and structural differences between glutamate and aspartate in intrinsically disordered proteins using experimental and computational methods.

bioRxiv · Aug 25, 2022Biophysics

Assessment of models for calculating the hydrodynamic radius of intrinsically disordered proteins

F. Pesce, E. A. Newcombe, P. Seiffert, E. E. Tranchant, J. G. Olsen, C. R. Grace, B. B. Kragelund, K. Lindorff-Larsen

The paper evaluates models for calculating the hydrodynamic radius of intrinsically disordered proteins using conformational ensembles validated by small-angle X-ray scattering and finds the Kirkwood-Riseman equation to be the most accurate.

bioRxiv · Jun 11, 2022Biophysics