Author

V. A. Lorenz-Fonfria

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· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:bacteria (other)· 1 Assay:imaging· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Chatterjee· 1 shared A. S. Chaudhari· 1 shared B. Schneider· 1 shared C. A. O. Domingos· 1 shared D. Sampedro· 1 shared E. Santamaria-Aranda· 1 shared G. Fuertes· 1 shared H. Kandori· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 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

1 shared paperBiophysics

A. Chatterjee

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiophysicsProtein SciencePeer-reviewedMar 16, 2023

Genetically encoded non-canonical amino acids reveal asynchronous dark reversion of chromophore, backbone and side-chains in EL222

A. S. Chaudhari, A. Chatterjee, C. A. O. Domingos…·G. Fuertes

This study uses genetically encoded amino acids to reveal asynchronous dark reversion dynamics in the EL222 photoreceptor, showing local structural changes precede global conformational relaxation.

DOI 10.1002/pro.4590

bacteria (other)proteomics

𝕏 PostBluesky

BiophysicsbioRxivJul 28, 2021

Retinal vibrations in bacteriorhodopsin are mechanically harmonic but electronically anharmonic: evidence from overtone and combination bands

V. A. Lorenz-Fonfria, K. Yagi, S. Ito, H. Kandori

The paper studies retinal vibrations in bacteriorhodopsin using IR and Raman spectroscopy, finding electronic anharmonicity explains overtone band intensities better than mechanical anharmonicity.

DOI 10.3389/fmolb.2021.749261

imagingexperimental assay

𝕏 PostBluesky

BiophysicsbioRxivMar 10, 2021

A photoswitchable helical peptide with light-controllable interface / transmembrane topology in lipidic membranes

M. Gutierrez-Salazar, E. Santamaria-Aranda, L. Schaar…·V. A. Lorenz-Fonfria

This paper introduces a photoswitchable helical peptide that can reversibly control its transmembrane (TM) and membrane interface (MI) topology using light.

DOI 10.1016/j.isci.2021.102771

experimental assay

𝕏 PostBluesky