Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Wenzhi Mao"'
Publikováno v:
BMC Bioinformatics, Vol 21, Iss 1, Pp 1-12 (2020)
Abstract Background Despite the great advance of protein structure prediction, accurate prediction of the structures of mainly β proteins is still highly challenging, but could be assisted by the knowledge of residue-residue pairing in β strands. P
Externí odkaz:
https://doaj.org/article/f31f9f862d7745a996acf0b35db3413a
Publikováno v:
BMC Bioinformatics, Vol 19, Iss 1, Pp 1-19 (2018)
Abstract Background Despite the rapid progress of protein residue contact prediction, predicted residue contact maps frequently contain many errors. However, information of residue pairing in β strands could be extracted from a noisy contact map, du
Externí odkaz:
https://doaj.org/article/4f37c0f169204a44a6c2bb3773f0f71b
Simulating the ion permeation and ion selection for a eukaryotic voltage-gated sodium channel NaVPaS
Publikováno v:
Protein & Cell, Vol 9, Iss 6, Pp 580-585 (2018)
Externí odkaz:
https://doaj.org/article/dacbf10e44084655a60fa1f1e7a98f17
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 16, Iss , Pp 503-510 (2018)
Information of residue-residue contacts is essential for understanding the mechanism of protein folding, and has been successfully applied as special topological restraints to simplify the conformational sampling in de novo protein structure predicti
Externí odkaz:
https://doaj.org/article/2bc99646b9834ebab20c611f28cdf300
Publikováno v:
PLoS Computational Biology, Vol 10, Iss 5, p e1003624 (2014)
The versatile functions of the heat shock protein 70 (Hsp70) family of molecular chaperones rely on allosteric interactions between their nucleotide-binding and substrate-binding domains, NBD and SBD. Understanding the mechanism of interdomain allost
Externí odkaz:
https://doaj.org/article/d98f90241b844fa9bd5d4bc99054589c
Publikováno v:
The International Journal of Advanced Manufacturing Technology. 121:8313-8327
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::906976e07aff9c269988724d22b28a9e
https://doi.org/10.1007/s00170-022-09900-y
https://doi.org/10.1007/s00170-022-09900-y
Publikováno v:
BMC Bioinformatics, Vol 21, Iss 1, Pp 1-12 (2020)
Background Despite the great advance of protein structure prediction, accurate prediction of the structures of mainly β proteins is still highly challenging, but could be assisted by the knowledge of residue-residue pairing in β strands. Previously
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc77cb869cebc539b8bf88ab7b30725a
http://link.springer.com/article/10.1186/s12859-020-3476-z
http://link.springer.com/article/10.1186/s12859-020-3476-z
Publikováno v:
Nature Machine Intelligence. 2:25-33
Predicting the structures of proteins from amino acid sequences is of great importance. Recently, the accuracy of de novo protein structure prediction has been substantially improved when assisted by information about the contact between residues, wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b836b0a3f76c3a045e0e145926f05c9b
https://doi.org/10.1038/s42256-019-0130-4
https://doi.org/10.1038/s42256-019-0130-4
Publikováno v:
Nature Machine Intelligence. 1:347-355
A typical approach to predicting unknown native structures of proteins is to assemble the amino acid residues (fragments) extracted from known structures. The quality of these extracted fragments, which are used to build protein-specific fragment lib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab6a566562ed373f4986430ccdf5456e
https://doi.org/10.1038/s42256-019-0075-7
https://doi.org/10.1038/s42256-019-0075-7
Publikováno v:
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal, Vol 16, Iss, Pp 503-510 (2018)
Computational and Structural Biotechnology Journal, Vol 16, Iss, Pp 503-510 (2018)
Information of residue-residue contacts is essential for understanding the mechanism of protein folding, and has been successfully applied as special topological restraints to simplify the conformational sampling in de novo protein structure predicti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a362685d1d710bdfbc512008dc0b2fdb
http://europepmc.org/articles/PMC6247404
http://europepmc.org/articles/PMC6247404