Professor, School of Life Sciences
University of Science and Technology of China
443 Huangshan Street
Hefei, Anhui 230027
P. R. China
Email: dlong[at]ustc.edu.cn
Personal Profile:
B.Sc. (2005) Wuhan University, Wuhan, Hubei, China
Ph.D. (2010) National University of Singapore, Singapore
2010 - 2012, Postdoctoral Fellow, Florida State University/National High Magnetic Field Laboratory, Tallahassee, Florida, United States
2012 - 2015, Postdoctoral Fellow, University of Toronto, Toronto, ON, Canada
2015 - present, Professor, University of Science and Technology of China, Hefei, China
Research Interest
• Investigation of the structures and dynamical properties of functionally important proteins and other macromolecules using NMR spectroscopy;
• Computational modeling/simulation of the structure and dynamics of macromolecular systems;
• Development of NMR and computational methodology for structural and dynamics studies of biomacromolecules.
Selected Publications:
1) D. Liu, Y. Mao, X. Gu, Y. Zhou, D. Long* (2021) Unveiling the invisible druggable conformations of GDP-bound inactive Ras. Proc. Natl. Acad. Sci. U.S.A. 118(11):e2024725118
2) X. Chen, H. Gao, D. Long* (2021) Millisecond Allosteric Dynamics of Activated Ras Reproduced with a Slowly Hydrolyzable GTP Analogue. ChemBioChem 22:1079-1083
3) D. Liu, X. Chen, D. Long* (2020) NMR-Derived Conformational Ensemble of State 1 of Activated Ras Reveals Insights into a Druggable Pocket. J. Phys. Chem. Lett. 11:3642-3646
4) X. Chen, H. Yao, H. Wang, Y. Mao, D. Liu, D. Long* (2019) Extending the lifetime of native GTP-bound Ras for site-resolved NMR measurements: Quantifying the allosteric dynamics. Angew. Chem. Int. Ed. 58:2730-2733
5) P. Cheng, D. Liu, P. X. Chee, D. Yang, D. Long* (2019) Atomistic Insights into the Functional Instability of the Second Helix of Fatty Acid Binding Protein. Biophys. J. 117:239-246
6) S. Li, R. Hu, H. Yao, D. Long, F. Luo, X. Zhou, X. Zhang, M. Liu, J. Zhu, Y. Yang (2018) Characterization of the interaction interface and conformational dynamics of human TGIF1 homeodomain upon the binding of consensus DNA. BBA - Proteins Proteom. 1866:1021-1028
7) H. Wang, S. Wang, C. Li, H. Li, Y. Mao, W. Liu, C. Xu*, D. Long* (2017) Probing transient release of membrane-sequestered tyrosine-based signaling motif by solution NMR spectroscopy. J. Phys. Chem. Lett. 8:3765-3769
8) Y. Mao, H. Yao, H. Wang, P. Cheng, D. Long* (2016) Microsecond timescale dynamics of GDP-bound Ras underlies the formation of novel inhibitor-binding pockets. Angew. Chem. Int. Ed. 55:15629-15632
9) D. Long,* F. Delaglio, A. Sekhar, L. E. Kay* (2015) Probing invisible, excited protein states by non-uniformly sampled pseudo-4D CEST spectroscopy. Angew. Chem. Int. Ed. 54:10507-10511
10) D. Long, A. Sekhar, L. E. Kay (2014) Triple resonance-based 13Cα and 13Cβ CEST experiments for studies of ms timescale dynamics in proteins. J. Biomol. NMR 60:203-208
11) D. Long, G. Bouvignies, L. E. Kay (2014) Measuring hydrogen exchange rates in invisible protein excited states. Proc. Natl. Acad. Sci. U.S.A. 111:8820-8825
12) D. Long, C. B. Marshall, G. Bouvignies, M. T. Mazhab-Jafari, M. J. Smith, M. Ikura, L. E. Kay. (2013) A comparative CEST NMR study of slow conformational dynamics of small GTPases complexed with GTP and GTP analogues. Angew. Chem. Int. Ed. 52:10771-10774
13) H. Sun, D. Long, R. Brüschweiler, V. Tugarinov. (2013) Carbon relaxation in 13Cα-Hα and 13Cα-Dα spin pairs as a probe of backbone dynamics in proteins. J. Phys. Chem. B 117:1308-1320
14) D. Long, R. Brüschweiler. (2013) Directional selection precedes conformational selection in ubiquitin-UIM binding. Angew. Chem. Int. Ed. 52: 3709-3711
15) D. Long, R. Brüschweiler. (2012) Structural and entropic allosteric signal transduction strength via correlated motions. J. Phys. Chem. Lett. 3:1722-1726
16) D. Long, R. Brüschweiler. (2011) Atomistic kinetic model for population shift and allostery in biomolecules. J. Am. Chem. Soc. 133:18999-19005
17) D. Long, D.W. Li, K. Walter, C. Griesinger, R. Brüschweiler. (2011) Toward a predictive understanding of slow methyl group dynamics in proteins. Biophys. J. 101:910-915
18) D. Long, R. Brüschweiler. (2011) In silico elucidation of the recognition dynamics of ubiquitin. PLoS Comput. Biol. 7: e1002035