Chaperone Domains, Redox Switches, Folding Switches

Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ. M.  Martinez-Yamout, G.B. Legge, O. Zhang, P.E. Wright and H.J. Dyson. (2000)  J. Mol. Biol. 300, 805-818.

Activation of the redox-regulated chaperone Hsp33 by domain unfolding.  P.C.F. Graf, M.A. Martinez-Yamout, S. VanHaerents, H. Lilie, H.J. Dyson and U. Jakob (2004).  J. Biol. Chem. 279, 20529-20538.

Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin.  Y. Kamikubo, R. DeGuzman, G. Kroon, S. Curriden, J. Neels, M.J. Churchill, P. Dawson, S. Oldziej, A. Jagielska, H.A. Scheraga, D.J. Loskutoff and H.J. Dyson (2004). Biochemistry 43, 6519-6534.

The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold.  H.-S. Won, L. Y. Low, R. N. De Guzman, M.A. Martinez-Yamout, U. Jakob and H.J. Dyson (2004).  J. Mol. Biol. 341, 893-899.

Backbone HN, N, Ca, C′ and Cb assignments of Escherichia coli SdiA1-171, the autoinducer binding domain of a quorum sensing protein. Y.Yao, M.A.Martinez-Yamout and H.J. Dyson (2005). J. Biomol. NMR 31, 373-374.

Structure of the Escherichia coli quorum sensing protein SdiA: activation of the folding switch by acyl homoserine lactones. Y. Yao, M.A. Martinez-Yamout, T.J. Dickerson, A.P. Brogan, P.E. Wright and H.J. Dyson (2006). J. Mol. Biol. 355, 262-273.

The reduced and denatured form of the somatomedin B domain of vitronectin refolds into a stable, biologically active form. Y. Kamikubo, G. Kroon, S.A. Curriden, H.J. Dyson and D.J. Loskutoff. Biochemistry 45, 3297-3306.

Localization of sites of interaction between p23 with Hsp90 in solution. M.A. Martinez-Yamout, R.P. Venkitakrishnan, N.E. Preece, G. Kroon, P.E. Wright and H.J. Dyson (2006). J. Biol. Chem. 281, 14457-14464.

Structure discrimination for the C-terminal domain of  E. coli trigger factor in solution. Y. Yao, G. Bhabha, M. Landes and H.J. Dyson (2007) J. Biomol. NMR 40, 23-30.

NMR detection of adventitious binding of xylose to the quorum-sensing protein SdiA of Escherichia coli. Y. Yao, T.J. Dickerson, M.S. Hixon and H. J. Dyson (2007). Bioorg. Med Chem. Lett. 17, 6202-6205.

Hydrogen-deuterium exchange strategy for delineation of contact sites in protein complexes. H.J. Dyson, M. Kostic, J. Liu and M.A. Martinez-Yamout (2008) FEBS Lett. 582, 1495-1500.

The client protein p53 forms a molten globule-like state in the presence of Hsp90. S.J. Park, M.A. Martinez-Yamout and H.J. Dyson (2011) Nature Struct. Mol. Biol. 18, 537-542.

Dynamic interaction of Hsp90 with its client protein p53. S.J. Park, M. Kostic and H.J. Dyson. (2011) J. Mol. Biol. 411, 158-173.

Homo-dimerization of the PAS-B domains of hypoxia inducible factors. J. Zhu, M.A. Martinez-Yamout, R. Cardoso, J. Yan, R.A. Love, N. Grodsky, A. Brooun and H.J. Dyson (2012) J. Phys. Chem. (in press)