Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Yanzhao Huang"'
Autor:
Hao Chen, Yunjie Zhao, Haotian Li, Dongyan Zhang, Yanzhao Huang, Qi Shen, Rachel Van Duyne, Fatah Kashanchi, Chen Zeng, Shiyong Liu
Publikováno v:
PLoS ONE, Vol 9, Iss 10, p e109154 (2014)
Most inhibitors of Cyclin-dependent kinase 2 (CDK2) target its ATP-binding pocket. It is difficult, however, to use this pocket to design very specific inhibitors because this catalytic pocket is highly conserved in the protein family of CDKs. Here w
Externí odkaz:
https://doaj.org/article/6e47d731620a40ffa641363ee5cd2c8e
Publikováno v:
PLoS ONE, Vol 8, Iss 10, p e75936 (2013)
In many protein-protein docking algorithms, binding site information is used to help predicting the protein complex structures. Using correct and accurate binding site information can increase protein-protein docking success rate significantly. On th
Externí odkaz:
https://doaj.org/article/7e4959415e22412d88af1d846dc6adf0
Publikováno v:
PLoS ONE, Vol 5, Iss 11, p e14138 (2010)
To understand how symmetric structures of many proteins are formed from asymmetric sequences, the proteins with two repeated beta-trefoil domains in Plant Cytotoxin B-chain family and all presently known beta-trefoil proteins are analyzed by structur
Externí odkaz:
https://doaj.org/article/19670637184d43c9b791052b7f949508
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 17, p 4116 (2019)
International Journal of Molecular Sciences
International Journal of Molecular Sciences
3D structures of RNAs are the basis for understanding their biological functions. However, experimentally solved RNA 3D structures are very limited in comparison with known RNA sequences up to now. Therefore, many computational methods have been prop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::901e71c25e7e1c5923990f8e786f1768
https://www.mdpi.com/1422-0067/20/17/4116
https://www.mdpi.com/1422-0067/20/17/4116
Autor:
Changjun Chen, Yanzhao Huang
Publikováno v:
Journal of Computational Chemistry. 37:1565-1575
Replica Exchange Molecular Dynamics (REMD) method is a powerful sampling tool in molecular simulations. Recently, we made a modification to the standard REMD method. It places some inactive replicas at different temperatures as well as the active rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::059e06a73a8bf4ac9c101877b470c2f0
https://doi.org/10.1002/jcc.24371
https://doi.org/10.1002/jcc.24371
Publikováno v:
Journal of Chemical Physics; 10/21/2014, Vol. 141 Issue 15, p1-8, 8p, 1 Diagram, 10 Graphs
Publikováno v:
Korean Journal of Chemical Engineering. 31:1082-1087
Acidic species were extracted from heavy crude oil by alcohol-alkali solution and ion exchange resin. The acidic species in the obtained extracts and extracted crude oil were characterized by negative-ion ESI FT-ICR MS. The analytical results indicat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::478380ce81379e96ebb5f5a01b49e7dd
https://doi.org/10.1007/s11814-014-0002-x
https://doi.org/10.1007/s11814-014-0002-x
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 31:206-214
Low sampling efficiency in conformational space is the well-known problem for conventional molecular dynamics. It greatly increases the difficulty for molecules to find the transition path to native state, and costs amount of CPU time. To accelerate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a364e691cafc40925c8879adc6a79abc
https://doi.org/10.1080/07391102.2012.698244
https://doi.org/10.1080/07391102.2012.698244
Publikováno v:
ACTA BIOPHYSICA SINICA. 27:395-402
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f4036b6088d9aa558a214c45edeb8ef8
https://doi.org/10.3724/sp.j.1260.2011.00395
https://doi.org/10.3724/sp.j.1260.2011.00395
Publikováno v:
Computational Biology and Chemistry. 33:325-328
Detection of foldable subunits in proteins is an important approach to understand their evolutions and find building motifs for de novo protein design. Using united-residue model, we simulated the folding of a six-helix protein with a length of 120 a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7d56303a2c8926a0b7db4cd80eec28e
https://doi.org/10.1016/j.compbiolchem.2009.06.001
https://doi.org/10.1016/j.compbiolchem.2009.06.001