Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Thierry Herning"'
Autor:
Stéphane Auvray, Jean-Claude Bernier, Thierry Engel, Marie-Paule Felder-Schmittbuhl, Marc Fontecave, Sébastien Forget, Jean-François Guillemoles, Thierry Herning, Norbert Hoffmann, Louis Le Sergeant d’Hendecourt, Jean-François Letard, Jacques Livage, Lionel Simonot
La lumière est partout et la chimie est partout. Mais ces deux entités se rencontrent-elles alors que l'une est immatérielle et l'autre constitutive de tous les objets? Oui, bien sûr! Cela s'est d'abord manifesté dans les sources naturelle
Autor:
Thierry Herning
Publikováno v:
Chimie et lumière
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3e3475e63ed89dc01f8c76f3f2f45534
https://doi.org/10.1051/978-2-7598-2508-0.c013
https://doi.org/10.1051/978-2-7598-2508-0.c013
Autor:
Jean-Claude Bernier, Thierry Herning, Stéphane Auvray, Jean-François Guillemoles, Sébastien Forget, Norbert Hoffmann, Louis Le Sergeant d’Hendecourt, Marc Fontecave, Jacques Livage, Marie-Paule Felder-Schmittbuhl, Thierry Engel, Lionel Simonot, Jean-François Letard
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd410552672f69c0e6b67a5e6003a408
https://doi.org/10.1051/978-2-7598-2508-0
https://doi.org/10.1051/978-2-7598-2508-0
Publikováno v:
Biochemistry. 30:9882-9891
The unfolding and refolding kinetics of six proline mutants of the human lysozyme (h-lysozyme) were carried out and compared to that of the wild-type protein. Our results show that the slow refolding phase observed in the h-lysozyme refolding kinetic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e55f040993fd502a1bdc523882c0a3e4
https://doi.org/10.1021/bi00105a011
https://doi.org/10.1021/bi00105a011
Publikováno v:
Analytica Chimica Acta. 244:207-213
The kinetics of specific DNA hybrid formation were monitored directly in solution. Detection was based on fluorescence polarization measurements of labelled oligonucleotides at different stages during the hybridization. The effect of mismatched base
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::54d4b672bbf92c5d3951b193b2c5e6be
https://doi.org/10.1016/s0003-2670(00)82500-3
https://doi.org/10.1016/s0003-2670(00)82500-3
Autor:
Koji Inaka, Masaaki Matsushima, Ryota Kuroki, Masakazu Kikuchi, Katsuhide Yutani, Thierry Herning
Publikováno v:
Biochemistry. 31(31)
It has been shown that protein stability can be modulated from site-directed mutations that affect the entropy of protein unfolding [Matthews, B. W., Nicholson, H., & Becktel, W. J. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 6663-6667]. However, the ef
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb3da4319fbd7b9900efaa0fd7b5bd7d
https://pubmed.ncbi.nlm.nih.gov/1643041
https://pubmed.ncbi.nlm.nih.gov/1643041