Zobrazeno 1 - 10
of 84
pro vyhledávání: '"Chigusa, Kobayashi"'
Publikováno v:
Biophysics and Physicobiology, Vol 20 (2023)
Externí odkaz:
https://doaj.org/article/016cd2ad2f6548c5aae9145a96c698e8
Publikováno v:
PLoS Computational Biology, Vol 18, Iss 4, p e1009578 (2022)
Residue-level coarse-grained (CG) models have become one of the most popular tools in biomolecular simulations in the trade-off between modeling accuracy and computational efficiency. To investigate large-scale biological phenomena in molecular dynam
Externí odkaz:
https://doaj.org/article/a853c17c404e4022af5f41aa197f3225
Publikováno v:
eLife, Vol 11 (2022)
Spike (S) protein is the primary antigenic target for neutralization and vaccine development for the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). It decorates the virus surface and undergoes large motions of its receptor binding doma
Externí odkaz:
https://doaj.org/article/e6d2fba80aa44428895594606307f61d
Autor:
Yu Shiozawa, Itoko Baba, Keiko Iwakoshi, Rina Nakamura, Yukiko Yamajima, Narue Sakamaki, Chigusa Kobayashi, Kenji Otsuka
Publikováno v:
Food Hygiene and Safety Science (Shokuhin Eiseigaku Zasshi). 64:94-99
Autor:
Takahiro Sasaki, Shoichi Tahara, Mari Morikawa, Tomoki Igarashi, Yuki Sadamasu, Keiko Ushiyama, Yukiko Yamajima, Chigusa Kobayashi
Publikováno v:
Food Hygiene and Safety Science (Shokuhin Eiseigaku Zasshi). 64:21-28
Publikováno v:
Biophysics and Physicobiology, Vol 16 (2019)
The dual-basin Gō-model is a structural-based coarsegrained model for simulating a conformational transition between two known structures of a protein. Two parameters are required to produce a dual-basin potential mixed using two single-basin potent
Externí odkaz:
https://doaj.org/article/796bd2ebdc77430593a9ef8e6ca3fa0e
Publikováno v:
Journal of Computational Chemistry.
Publikováno v:
Journal of Chemical Theory and Computation. 17:5312-5321
In recent years, molecular dynamics (MD) simulations with larger time steps have been performed with the hydrogen-mass-repartitioning (HMR) scheme, where the mass of each hydrogen atom is increased to reduce high-frequency motion while the mass of a
Publikováno v:
Seibutsu Butsuri. 62:298-300
Publikováno v:
Journal of Chemical Information and Modeling. 61:2427-2443
Large-scale conformational transitions in multi-domain proteins are often essential for their functions. To investigate the transitions, it is necessary to explore multiple potential pathways, which involve different intermediate structures. Here, we