Zobrazeno 1 - 6
of 6
pro vyhledávání: '"yoann cote"'
Publikováno v:
Biophysical Journal
Biophysical Journal, Biophysical Society, 2017, 112 (12), pp.2575-2588. ⟨10.1016/j.bpj.2017.05.018⟩
Biophysical Journal, 2017, 112 (12), pp.2575-2588. ⟨10.1016/j.bpj.2017.05.018⟩
Biophysical Journal, Biophysical Society, 2017, 112 (12), pp.2575-2588. ⟨10.1016/j.bpj.2017.05.018⟩
Biophysical Journal, 2017, 112 (12), pp.2575-2588. ⟨10.1016/j.bpj.2017.05.018⟩
PMC5479146; Molecular dynamics (MD) simulations and far-infrared (far-IR) spectroscopy were combined to study peptide binding by the second PDZ domain (PDZ1) of MAGI1, which has been identified as an important target for the Human Papilloma Virus. PD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22c1129f69f92388b4a7b63633f62b64
https://doi.org/10.1016/j.bpj.2017.05.018
https://doi.org/10.1016/j.bpj.2017.05.018
Publikováno v:
ACS Chemical Neuroscience
ACS Chemical Neuroscience, 2018, 9 (5), pp.1051-1065. ⟨10.1021/acschemneuro.7b00446⟩
ACS Chemical Neuroscience, 2018, 9 (5), pp.1051-1065. ⟨10.1021/acschemneuro.7b00446⟩
alpha-Synuclein (alphaS) is a major constituent of Lewy bodies, the insoluble aggregates that are the hallmark of one of the most prevalent neurodegenerative disorders, Parkinson's disease (PD). The vast majority of experiments in vitro and in vivo p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f30bc6c87d2163119d5cc0ae11615f6
https://europepmc.org/articles/PMC5955826/
https://europepmc.org/articles/PMC5955826/
Publikováno v:
Proceedings of the National Academy of Sciences. 107:19844-19849
Structural fluctuations of a protein are essential for the function of native proteins and for protein folding. To understand how the main chain in the native state of a protein fluctuates on different time scales, we examined the rotational correlat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2844acc25fa650e0b0461909a2c8dd62
https://doi.org/10.1073/pnas.1013674107
https://doi.org/10.1073/pnas.1013674107
Publikováno v:
The journal of physical chemistry letters. 6(6)
A fundamental open problem in biophysics is how the folded structure of the main chain (MC) of a protein is determined by the physics of the interactions between the side-chains (SCs). All-atom molecular dynamics simulations of a model protein (Trp-c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39d2843998c0f55ca4306cbb92f1357f
https://pubmed.ncbi.nlm.nih.gov/25866611
https://pubmed.ncbi.nlm.nih.gov/25866611
Publikováno v:
The journal of physical chemistry. C, Nanomaterials and interfaces, vol 118, iss 29
Cote, Y; Fu, IW; Dobson, ET; Goldberger, JE; Nguyen, HD; & Shen, JK. (2014). Mechanism of the pH-controlled self-assembly of nanofibers from peptide amphiphiles. Journal of Physical Chemistry C, 118(29), 16272-16278. doi: 10.1021/jp5048024. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/99w367nk
ResearcherID
The Journal of Physical Chemistry. C, Nanomaterials and Interfaces
Cote, Y; Fu, IW; Dobson, ET; Goldberger, JE; Nguyen, HD; & Shen, JK. (2014). Mechanism of the pH-controlled self-assembly of nanofibers from peptide amphiphiles. Journal of Physical Chemistry C, 118(29), 16272-16278. doi: 10.1021/jp5048024. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/99w367nk
ResearcherID
The Journal of Physical Chemistry. C, Nanomaterials and Interfaces
Stimuli-responsive, self-assembling nanomaterials hold a great promise to revolutionize medicine and technology. However, current discovery is slow and often serendipitous. Here we report a multiscale modeling study to elucidate the pH-controlled sel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81ae878259c4ed24a9489296a3cac9da
https://escholarship.org/uc/item/99w367nk
https://escholarship.org/uc/item/99w367nk
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2012, 109, pp.10346--10351. 〈10.1073/pnas.1207083109〉
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2012, 109, pp.10346--10351. ⟨10.1073/pnas.1207083109⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2012, 109, pp.10346--10351. 〈10.1073/pnas.1207083109〉
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2012, 109, pp.10346--10351. ⟨10.1073/pnas.1207083109⟩
Structural fluctuations of a protein are essential for a protein to function and fold. By using molecular dynamics (MD) simulations of the model α/β protein VA3 in its native state, the coupling between the main-chain (MC) motions [represented by c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a576e44ae57fcd8517d6ac56c12d77d3
https://europepmc.org/articles/PMC3387131/
https://europepmc.org/articles/PMC3387131/