Zobrazeno 1 - 10
of 67
pro vyhledávání: '"George Chikenji"'
Publikováno v:
PLoS Computational Biology, Vol 20, Iss 8, p e1012282 (2024)
A protein superfold is a type of protein fold that is observed in at least three distinct, non-homologous protein families. Structural classification studies have revealed a limited number of prevalent superfolds alongside several infrequent occurrin
Externí odkaz:
https://doaj.org/article/da98752546254eb9b6f4ff92b6571b29
Publikováno v:
Molecules, Vol 27, Iss 11, p 3547 (2022)
Superfolds are folds commonly observed among evolutionarily unrelated multiple superfamilies of proteins. Since discovering superfolds almost two decades ago, structural rules distinguishing superfolds from the other ordinary folds have been explored
Externí odkaz:
https://doaj.org/article/f643443fd078461bb025c5a23d864422
Publikováno v:
PLoS ONE, Vol 16, Iss 8, p e0256895 (2021)
A wide range of de novo design of αβ-proteins has been achieved based on the design rules, which describe secondary structure lengths and loop torsion patterns favorable for design target topologies. This paper proposes design rules for register sh
Externí odkaz:
https://doaj.org/article/f22745609f194d33acfd0ee5a8620f6b
Publikováno v:
PLoS ONE, Vol 9, Iss 9, p e107959 (2014)
It has been known that topologically different proteins of the same class sometimes share the same spatial arrangement of secondary structure elements (SSEs). However, the frequency by which topologically different structures share the same spatial a
Externí odkaz:
https://doaj.org/article/148364029eb4436db2190b2b1727fa9b
In this study, we propose an analytic statistical mechanics approach to solve a fundamental problem in biological physics called protein design. Protein design is an inverse problem of protein structure prediction, and its solution is the amino acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f9762889f240b847603b4f0f47ea325
Autor:
Rie Koga, Toshimichi Fujiwara, George Chikenji, Toshihiko Sugiki, Nobuyasu Koga, Naohiro Kobayashi, Toshio Nagashima, Shintaro Minami
Most naturally occurring protein folds have likely been discovered1–3. The question is whether natural evolution has exhaustively sampled almost all possible protein folds4, or whether a large fraction of the possible folds remains unexplored5–7.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::610714da657d27c15655a9ea580858b2
https://doi.org/10.1101/2021.08.06.455475
https://doi.org/10.1101/2021.08.06.455475
Publikováno v:
Physical review. E. 104(1-1)
Protein design is the inverse approach of the three-dimensional (3D) structure prediction for elucidating the relationship between the 3D structures and amino acid sequences. In general, the computation of the protein design involves a double loop: a
Publikováno v:
Bioinformatics. 34:3324-3331
Motivation Protein structure alignment is a significant tool to understand evolutionary processes and physicochemical properties of proteins. Important targets of structure alignment are not only monomeric but also oligomeric proteins that sometimes
Publikováno v:
Protein Science. 26:2257-2267
In protein structures, the fold is described according to the spatial arrangement of secondary structure elements (SSEs: α-helices and β-strands) and their connectivity. The connectivity or the pattern of links among SSEs is one of the most importa
Autor:
Rie Koga, George Chikenji, Toshihiko Sugiki, Shintaro Minami, Nobuyasu Koga, Naohiro Kobayashi
Publikováno v:
Biophysical Journal. 118:43a