Author

P. Falson

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:cryo-EM· 2 Approach:experimental assay· 2 Research Focus:protein structure prediction· 2 Research Focus:chromatin & epigenetic regulation· 1 Approach:microscopy & imaging analysis· 1 Assay:structural biology· 1

Frequent Co-Authors

v. Chaptal· 3 shared A. Gobet· 2 shared J. Martin· 2 shared X. Robert· 2 shared C. Orelle· 1 shared E. Bettler· 1 shared E. Zarkadas· 1 shared G. Schoehn· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 39 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

3 shared papersBiophysics

v. Chaptal

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

R6G narrows BmrA conformational spectrum for a more efficient use of ATP

A. Gobet, L. Moissonnier, E. Zarkadas, S. Magnard, E. Bettler, J. Martin, R. Terreux, G. Schoehn, C. Orelle, J.-M. Jault, P. Falson, v. Chaptal

This study shows that Rhodamine6G binding to BmrA narrows its conformational spectrum, enhancing ATP-dependent transport efficiency.

bioRxiv · Mar 15, 2024 · PreprintBiochemistry

Collinearity of alpha-helices or beta strands in membrane proteins causes a characteristic peak centred on 4.9 A resolution in diffraction intensity profiles, inducing higher diffraction anisotropy

J. Martin, X. Robert, P. Gouet, P. Falson, v. Chaptal

bioRxiv · Dec 7, 2021 · PreprintBiophysics

Nanodisc, amphipol or detergent belts in cryoEM reconstructions of membrane proteins are similar and correspond to a common ordered solvent layer

V. Zampieri, A. Gobet, X. Robert, P. Falson, v. Chaptal

The paper compares belt structures in cryo-EM reconstructions of membrane proteins solved in nanodiscs, amphipols, or detergents, finding they are similar and represent a common ordered solvent layer.

bioRxiv · Dec 10, 2020Biophysics