Zobrazeno 1 - 3
of 3
pro vyhledávání: '"M. Saber Naderi"'
Publikováno v:
Physical Biology, 15(6). IOP PUBLISHING LTD
Physical Biology, 15(6):066010. Institute of Physics
Physical biology
Physical Biology, 15(6):066010. Institute of Physics
Physical biology
By means of replica exchange molecular dynamics simulations we investigate how the length of a silk-like, alternating diblock oligopeptide influences its secondary and quaternary structure. We carry out simulations for two protein sizes consisting of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14eb0eb4677a7b928990b0e51f440409
https://dspace.library.uu.nl/handle/1874/376664
https://dspace.library.uu.nl/handle/1874/376664
Publikováno v:
Soft Matter, 10(29), 5362. The Royal Society of Chemistry
We perform Replica Exchange Molecular Dynamics (REMD) simulations on a silk-like protein design with amino-acid sequence [(Gly-Ala)3-Gly- Glu]5 to investigate the stability of a single protein, a dimer, a trimer and a tetramer made up of these protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f47d248e28174f131a39bacae3bf63b6
https://dspace.library.uu.nl/handle/1874/306975
https://dspace.library.uu.nl/handle/1874/306975
Autor:
Emilie Pouget, Paul van der Schoot, M. Paul Lettinga, Pierre Ballesta, Eric Grelet, M. Saber Naderi
Publikováno v:
Physical Review Letters, 111(3), 037801/1. American Physical Society
Physical Review Letters, 111(3):037801, 1-5. American Physical Society
Physical review letters 111(3), 037801 (2013). doi:10.1103/PhysRevLett.111.037801
Physical Review Letters
Physical Review Letters, American Physical Society, 2013, 111 (037801), pp. 1-5. ⟨10.1103/PhysRevLett.111.037801⟩
Physical Review Letters, 111(3):037801, 1-5. American Physical Society
Physical review letters 111(3), 037801 (2013). doi:10.1103/PhysRevLett.111.037801
Physical Review Letters
Physical Review Letters, American Physical Society, 2013, 111 (037801), pp. 1-5. ⟨10.1103/PhysRevLett.111.037801⟩
International audience; We report on single-particle dynamics of strongly interacting filamentous fd virus particles in the liquidcrystalline columnar state in aqueous solution. From fluorescence microscopy, we find that rare, discrete events take pl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a14512a3ebb2b5a200b89362cb0e5c4
https://dspace.library.uu.nl/handle/1874/291394
https://dspace.library.uu.nl/handle/1874/291394