Biochemistry at Univ. Maryland
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David Fushman

David Fushman
Associate Professor
phone: 301.405.3461
fax: 301.314.0386

Lab web site

Chem. and Biochem. web site

Research Summary

Development and application of new experimental and theoretical approaches to study structural properties, dynamics, interactions, and regulation in multidomain systems. Polyubiquitin signaling. Structure determination and analysis of proteins, nuclear magnetic resonance (NMR) and relaxation, computational biology, molecular dynamics simulations, physical and mathematical modeling.

Selected Recent Publications

M. Sadqi, D. Fushman, V. Munoz, “Atom-by-atom analysis of global downhill protein folding,” Nature 442, 317-321 (2006).

R. Varadan, M. Assfalg, S. Raasi, C. Pickart, D. Fushman, “Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain,” Molecular Cell 18, 687-698 (2005).

S. Raasi, R. Varadan, D. Fushman, C. M. Pickart, “Diverse polyubiquitin interaction properties of ubiquitin-associated domains,” Nature Struct. Mol. Biol. 12, 708-714 (2005).

Verma et al., “Ubistatins Inhibit Proteasome-Dependent Degradation by Binding the Ubiquitin Chain”, Science 306, 117-120 (2004).

R. Varadan, M. Assfalg, A. Haririnia, S. Raasi, C. Pickart, D. Fushman, “Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling,” J. Biol. Chem. 279, 7055-7063 (2004).

D. Fushman, R. Varadan, M. Assfalg, O. Walker “Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements,” Progress in NMR Spectroscopy 44, 189-214 (2004).

J. B. Hall and D. Fushman, “Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: Differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G,” J. Biomol. NMR 27, 261-275 (2003).

R. Varadan, O. Walker, C. Pickart, D. Fushman, “Structural properties of polyubiquitin chains in solution,” J. Mol. Biol. 324, 637-647 (2002).


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