Zobrazeno 1 - 10
of 69
pro vyhledávání: '"Víctor A. Lórenz-Fonfría"'
Autor:
Èric Catalina-Hernández, Mario López-Martín, David Masnou-Sánchez, Marco Martins, Victor A. Lorenz-Fonfria, Francesc Jiménez-Altayó, Ute A. Hellmich, Hitoshi Inada, Antonio Alcaraz, Yuji Furutani, Alfons Nonell-Canals, Jose Luis Vázquez-Ibar, Carmen Domene, Rachelle Gaudet, Alex Perálvarez-Marín
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 23, Iss , Pp 473-482 (2024)
TRP channels are important pharmacological targets in physiopathology. TRPV2 plays distinct roles in cardiac and neuromuscular function, immunity, and metabolism, and is associated with pathologies like muscular dystrophy and cancer. However, TRPV2 p
Externí odkaz:
https://doaj.org/article/fec8ab2a92ba4a038f5fbb653e8b027b
Autor:
Yingliang Liu, Aditya S. Chaudhari, Aditi Chatterjee, Prokopis C. Andrikopoulos, Alessandra Picchiotti, Mateusz Rebarz, Miroslav Kloz, Victor A. Lorenz-Fonfria, Bohdan Schneider, Gustavo Fuertes
Publikováno v:
Biomolecules, Vol 13, Iss 1, p 161 (2023)
Time-resolved femtosecond-stimulated Raman spectroscopy (FSRS) provides valuable information on the structural dynamics of biomolecules. However, FSRS has been applied mainly up to the nanoseconds regime and above 700 cm−1, which covers only part o
Externí odkaz:
https://doaj.org/article/dc5ee58bfcfb49ceb98894d343d32818
Autor:
Víctor A. Lórenz-Fonfría, Mónica Gutiérrez-Salazar, Eduardo Santamaría-Aranda, Jesús Salgado, Diego Sampedro
The spontaneous (translocon-unassisted) folding/insertion of helical transmembrane (TM) protein fragments into lipid bilayers is driven by three sequential equilibria: solution-to-membrane interface (MI) partition, unstructured-to-helical folding, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_____10175::f393259d526919afd7b78518fc163ad6
https://investigacion.unirioja.es/documentos/641afdb7124b445f6ae671e4
https://investigacion.unirioja.es/documentos/641afdb7124b445f6ae671e4
Autor:
Víctor A. Lórenz-Fonfría
Publikováno v:
Chemical Reviews. 120:3466-3576
Infrared difference spectroscopy probes vibrational changes of proteins upon their perturbation. Compared with other spectroscopic methods, it stands out by its sensitivity to the protonation state, H-bonding, and the conformation of different groups
Vibrations of the chromophore in the membrane protein bacteriorhodopsin (BR), a protonated Schiff base retinal, have been studied for decades, both by resonance Raman and by infrared (IR) difference spectroscopy. In spite the light-induced IR differe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e1e33b7f5a7c66582f53c092235b0ef4
https://doi.org/10.1101/2021.07.28.454158
https://doi.org/10.1101/2021.07.28.454158
Autor:
Jesús Salgado, Diego Sampedro, Eduardo Santamaría-Aranda, Mónica Gutiérrez-Salazar, Víctor A. Lórenz-Fonfría, Louise Schaar
According to the three-step model, the spontaneous insertion and folding of helical transmembrane (TM) polypeptides into lipid bilayers is driven by three sequential equilibria: solution-to-membrane interface (MI) partition, unstructured-to-helical f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::058feab97d6558ce1deb05ea4eba7bb5
https://doi.org/10.1101/2021.03.10.434736
https://doi.org/10.1101/2021.03.10.434736
Autor:
Yuji Furutani, Ryuichiro Ishitani, Osamu Nureki, Víctor A. Lórenz-Fonfría, Tetsunari Kimura, Hideyoshi Motoki, Masahiro Higashi, Shintaro Douki
Publikováno v:
The Journal of Physical Chemistry B. 122:9681-9696
Magnesium ions (Mg2+) are crucial for various biological processes. A bacterial Mg2+ channel, MgtE, tightly regulates the intracellular Mg2+ concentration. Previous X-ray crystal structures showed that MgtE forms a dimeric structure composed of a tot
Autor:
Tom Resler, Víctor A. Lórenz-Fonfría, Ramona Schlesinger, Franziska Pranga-Sellnau, Mattia Saita, Joachim Heberle
Publikováno v:
Journal of the American Chemical Society. 140:9899-9903
Channelrhodopsins (ChRs) are light-gated cation channels. In spite of their wide use to activate neurons with light, the photocurrents of ChRs rapidly decay in intensity under both continuous illum...
Publikováno v:
Applied Spectroscopy. 72:956-963
Fourier transform infrared (FT-IR) difference absorption spectroscopy is a common method for studying the structural and dynamical aspects behind protein function. In particular, the 2800–1800 cm−1 spectral range has been used to obtain informati
Autor:
Roland R. Netz, Matthias Heyden, Víctor A. Lórenz-Fonfría, Jan O. Daldrop, Joachim Heberle, Mattia Saita
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-7 (2018)
Nature Communications
Nature Communications
Infrared continuum bands that extend over a broad frequency range are a key spectral signature of protonated water clusters. They are observed for many membrane proteins that contain internal water molecules, but their microscopic mechanism has remai