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. |
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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,”
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in macromolecules by using spin-relaxation and residual dipolar coupling measurements,”
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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,
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