Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Olivier Bouffioux"'
Publikováno v:
Journal of Molecular Graphics and Modelling. 22:11-21
Few structures of membrane proteins are known and their relationships with the membrane are unclear. In a previous report, 20 X-ray structures of transmembrane proteins were analyzed in silico for their orientation in a 36 A-thick membrane [J. Mol. G
Autor:
Hary Razafindralambo, Michel Paquot, Philippe Jacques, Robert Brasseur, Magali Deleu, Choukri Hbid, Philippe Thonart, Olivier Bouffioux
Publikováno v:
Langmuir. 19:3377-3385
Modeling analysis was used to understand the molecular mechanisms of the biological activities of surfactin, in particular, its hemolytic activity. This study highlights the importance of the fatty acid chain hydrophobicity of the surfactin on its ac
Publikováno v:
Proteins: Structure, Function, and Genetics. 43:28-36
Pex are created to extract numeric and string descriptions of protein structures from PDB files. This concerns covalent bond lengths and angles, secondary structures, residues in interaction, H-bond lengths and geometry, etc. Several kinds of Pex are
Autor:
Olivier Bouffioux, Alain Prochiantz, Jacques J. Picard, Chloë Shaw-Jackson, Robert Brasseur, Christelle Matis, Marie-Paule Mingeot-Leclercq, Geneviève Dom, René Rezsohazy
Publikováno v:
Nucleic Acids Research, Vol. 31, no. 2, p. 556-561 (2003)
Several homeodomains and homeodomain-containing proteins enter live cells through a receptor- and energy-independent mechanism. Translocation through biological membranes is conferred by the third alpha-helix of the homeodomain, also known as Penetra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0d84a9db473669e9d41d4e3d4b3fa70
https://hdl.handle.net/2078.1/9353
https://hdl.handle.net/2078.1/9353