Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Xiang-Hua Dou"'
Autor:
Jia-Feng Yu, Xiang-Hua Dou, Yu-Jie Sha, Chun-Ling Wang, Hong-Bo Wang, Yi-Ting Chen, Feng Zhang, Yaoqi Zhou, Ji-Hua Wang
Publikováno v:
BMC Bioinformatics, Vol 18, Iss 1, Pp 1-5 (2017)
Abstract Background Intrinsically unstructured or disordered proteins function via interacting with other molecules. Annotation of these binding sites is the first step for mapping functional impact of genetic variants in coding regions of human and
Externí odkaz:
https://doaj.org/article/76c7646075334960bb6847c3fc6902b7
Publikováno v:
Journal of Chemical Information and Modeling. 55:1261-1270
The composition and sequence order of amino acid residues are the two most important characteristics to describe a protein sequence. Graphical representations facilitate visualization of biological sequences and produce biologically useful numerical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cd3b16681496fef53bb83cc1f222665
https://doi.org/10.1021/ci500577m
https://doi.org/10.1021/ci500577m
Publikováno v:
2009 International Conference on Computational Intelligence and Natural Computing.
Based on MD simulations, we calculated the conformational entropies of a designed 10-residue peptide, or the mini-protein Chignolin’s eight residues (2-9) at four different temperature. Our results show that five conformational entropies of Chignol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6cb2ec3bc196b71803bc568536631edf
https://doi.org/10.1109/cinc.2009.53
https://doi.org/10.1109/cinc.2009.53
Publikováno v:
2008 2nd International Conference on Bioinformatics and Biomedical Engineering.
The B1 domain of protein G is a paradigm for kinetics studies. In this work, the protein structure of GB1 is modeled as an unweighted amino acid network. We find that the unweighted amino acid network is the typical property of small-world network. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0741e7e9326b619d9a7eafb82250226d
https://doi.org/10.1109/icbbe.2008.57
https://doi.org/10.1109/icbbe.2008.57
Publikováno v:
Journal of biomolecular structuredynamics. 25(6)
Forty nine molecular dynamics simulations of unfolding trajectories of the segment B1 of streptococcal protein G (GB1) provide a direct demonstration of the diversity of unfolding pathway and give a statistically utmost unfolding pathway under the ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d325374f0d681a1b460a97665e06b59
https://pubmed.ncbi.nlm.nih.gov/18399694
https://pubmed.ncbi.nlm.nih.gov/18399694
Publikováno v:
2009 International Conference on Computational Intelligence & Natural Computing; 2009, p495-498, 4p