Haipeng Gong
Affiliations: | 2000-2007 | Program of Molecular Biophysics | Johns Hopkins University, Baltimore, MD |
2007-2009 | Department of Chemistry | University of Chicago, Chicago, IL | |
2009- | School of Life Sciences | Tsinghua National University, Beijing, Beijing Shi, China |
Website:
http://structpred.life.tsinghua.edu.cnGoogle:
"Haipeng Gong"Mean distance: (not calculated yet)
Parents
Sign in to add mentorKarl F. Freed | post-doc | 2007-2009 | Chicago |
Tobin R. Sosnick | post-doc | 2007-2009 | Chicago |
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Publications
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Li Y, Gong H. (2022) Identifying a Feasible Transition Pathway between Two Conformational States for a Protein. Journal of Chemical Theory and Computation |
Ding W, Xu Q, Liu S, et al. (2021) SAMF: a Self-adaptive Protein Modeling Framework. Bioinformatics (Oxford, England) |
Ding W, Gong H. (2020) Predicting the Real-Valued Inter-Residue Distances for Proteins. Advanced Science (Weinheim, Baden-Wurttemberg, Germany). 7: 2001314 |
Ding W, Mao W, Shao D, et al. (2018) DeepConPred2: An Improved Method for the Prediction of Protein Residue Contacts. Computational and Structural Biotechnology Journal. 16: 503-510 |
Xiong D, Mao W, Gong H. (2017) Predicting the helix-helix interactions from correlated residue mutations. Proteins |
Gong H, Zhang S, Wang J, et al. (2016) Constructing Structure Ensembles of Intrinsically Disordered Proteins from Chemical Shift Data. Journal of Computational Biology : a Journal of Computational Molecular Cell Biology. 23: 300-10 |
Zhang S, Zhou J, Hu H, et al. (2015) A deep learning framework for modeling structural features of RNA-binding protein targets. Nucleic Acids Research |
Liu Y, Haddadian E, Sosnick TR, et al. (2013) A novel implicit solvent model for simulating the molecular dynamics of RNA. Biophysical Journal. 105: 1248-57 |
Liu Y, Gong H. (2012) Using the unfolded state as the reference state improves the performance of statistical potentials. Biophysical Journal. 103: 1950-9 |
Haddadian EJ, Gong H, Jha AK, et al. (2011) Automated real-space refinement of protein structures using a realistic backbone move set. Biophysical Journal. 101: 899-909 |