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of 62
pro vyhledávání: '"Charles H. Robert"'
Autor:
Anne-Elisabeth Molza, Yvonne Westermaier, Magali Moutte, Pierre Ducrot, Claudia Danilowicz, Veronica Godoy-Carter, Mara Prentiss, Charles H. Robert, Marc Baaden, Chantal Prévost
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Recent advances in structural biophysics and integrative modelling methods now allow us to decipher the structures of large macromolecular assemblies. Understanding the dynamics and mechanisms involved in their biological function requires rigorous i
Externí odkaz:
https://doaj.org/article/cbb8e3ac6752421ebb24cb7700b5bdd9
Publikováno v:
IUCrJ, Vol 2, Iss 6, Pp 643-652 (2015)
Protein interactions are essential in all biological processes. The changes brought about in the structure when a free component forms a complex with another molecule need to be characterized for a proper understanding of molecular recognition as wel
Externí odkaz:
https://doaj.org/article/690dc8ee6ce7415699362ddf4771cdde
Autor:
Anne-Elisabeth Molza, Yvonne Westermaier, Magali Moutte, Pierre Ducrot, Claudia Danilowicz, Veronica Godoy-Carter, Mara Prentiss, Charles H. Robert, Marc Baaden, Chantal Prévost
Publikováno v:
Frontiers in molecular biosciences. 9
Recent advances in structural biophysics and integrative modelling methods now allow us to decipher the structures of large macromolecular assemblies. Understanding the dynamics and mechanisms involved in their biological function requires rigorous i
Publikováno v:
Bio-protocol
Bio-protocol, Bio-protocol LCC, 2021, 11 (14), ⟨10.21769/BioProtoc.4097⟩
Bio Protoc
Bio-protocol, Bio-protocol LCC, 2021, 11 (14), ⟨10.21769/BioProtoc.4097⟩
Bio Protoc
Protein filaments are dynamic entities that respond to external stimuli by slightly or substantially modifying the internal binding geometries between successive protomers. This results in overall changes in the filament architecture, which are diffi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::720ca1aa2045159c7caf5e929048f44c
https://hal.archives-ouvertes.fr/hal-03365534/file/Boyer_Bioprotocol_author-version.pdf
https://hal.archives-ouvertes.fr/hal-03365534/file/Boyer_Bioprotocol_author-version.pdf
Autor:
Charles H. Robert
Reproduction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b9b50391705defac97d98a4f72d6c78
Publikováno v:
Biochemistry (mosc.)
Biochemistry (mosc.), MAIK Nauka/Interperiodica : Springer Science+Business Media LLC, 2017, ⟨10.1021/acs.biochem.6b00988⟩
Biochemistry (mosc.), MAIK Nauka/Interperiodica : Springer Science+Business Media LLC, 2017, ⟨10.1021/acs.biochem.6b00988⟩
International audience; Although they play a significant part in the regulation of microtubule structure, dynamics and function, the disordered C-terminal tails of tubulin remain invisible to experimental structural methods and do not appear in the c
Publikováno v:
Journal of Computational Chemistry. 37:739-752
The number of local minima of the potential energy landscape (PEL) of molecular systems generally grows exponentially with the number of degrees of freedom, so that a crucial property of PEL exploration algorithms is their ability to identify local m
Publikováno v:
Journal of Computational Chemistry. 36:1213-1231
We present novel algorithms and software addressing four core problemsin computational structural biology, namely analyzing a conformationalensemble, comparing two conformational ensembles, analyzing a sampledenergy landscape, and comparing two sampl