Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Koya Sakuma"'
Autor:
Koya Sakuma, Shintaro Minami
Publikováno v:
BMC Bioinformatics, Vol 22, Iss 1, Pp 1-15 (2021)
Abstract Background The design of protein structures from scratch requires special attention to the combination of the types and lengths of the secondary structures and the loops required to build highly designable backbone structure models. However,
Externí odkaz:
https://doaj.org/article/39618de2f53840cfb7f595720f46343f
Publikováno v:
Biology, Vol 12, Iss 2, p 182 (2023)
AlphaFold2 (AF2) is a protein structure prediction program which provides accurate models. In addition to predicting structural domains, AF2 assigns intrinsically disordered regions (IDRs) by identifying regions with low prediction reliability (pLDDT
Externí odkaz:
https://doaj.org/article/7f6e54e7d0b04d78a43e3548a82f9d79
Autor:
Koya Sakuma
Publikováno v:
Biophysics and Physicobiology, Vol 18 (2021)
ABEGO is a coarse-grained representation for polypeptide backbone dihedral angles. The Ramachandran map is divided into four segments denoted as A, B, E, and G to represent the local conformation of polypeptide chains in the character strings. Al
Externí odkaz:
https://doaj.org/article/8cba2bed42ed468dbbe2025136332555
AlphaFold protein structure database (AlphaFold DB) archives a vast number of predicted models. We conducted systematic data mining against AlphaFold DB and discovered an uncharacterized P-loop NTPase family. The structure of the protein family was s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fbd5e4f66a178699d8dd9143262374de
https://doi.org/10.1101/2023.02.19.529160
https://doi.org/10.1101/2023.02.19.529160
Autor:
Shintaro Minami, Koya Sakuma
Publikováno v:
BMC Bioinformatics, Vol 22, Iss 1, Pp 1-15 (2021)
BMC Bioinformatics
BMC Bioinformatics
Background The design of protein structures from scratch requires special attention to the combination of the types and lengths of the secondary structures and the loops required to build highly designable backbone structure models. However, it is di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8db19788f5611c834cc5fd2ca99c6c9
https://doaj.org/article/39618de2f53840cfb7f595720f46343f
https://doaj.org/article/39618de2f53840cfb7f595720f46343f
Autor:
Takeshi Murata, Nobuyasu Koga, Toshihiko Sugiki, Rie Koga, Kano Suzuki, Toshimichi Fujiwara, Naoya Kobayashi, Takahiro Kosugi, Koya Sakuma, Toshio Nagashima, Naohiro Kobayashi
A wide range of de novo protein structure designs have been achieved, but the complexity of naturally occurring protein structures is still far beyond these designs. To expand the diversity and complexity of de novo designed protein structures, we so
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f267d06870edbe50e080cc12b004b1bb
https://doi.org/10.1101/2021.07.14.449347
https://doi.org/10.1101/2021.07.14.449347
Autor:
Takeshi Murata, Takahiro Kosugi, Nobuyasu Koga, Naohiro Kobayashi, Naoya Kobayashi, Rie Koga, Koya Sakuma, Toshihiko Sugiki, Kano Suzuki
Publikováno v:
Biophysical Journal. 118:43a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::34ab87a1e94b40c19b06f59370cea47b
https://doi.org/10.1016/j.bpj.2019.11.414
https://doi.org/10.1016/j.bpj.2019.11.414