Protein Dynamics

¹H, ¹³C and ¹⁵N NMR backbone assignments of 25.5 kDa metallo-b-lactamase from Bacteroides fragilis. S.D.B. Scrofani, P.E. Wright and H.J. Dyson (1998) J. Biomol. NMR 12, 201-202.

The identification of metal-binding ligand residues in metalloproteins using nuclear magnetic resonance spectroscopy. S.D.B. Scrofani, P.E. Wright and H.J. Dyson (1998) Protein Sci. 7, 2476-2479.

Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2. B.M. Duggan, H.J. Dyson & P.E. Wright (1999) Eur. J. Biochem. 265, 539-548.

NMR characterization of the metallo-b-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: Role of an active-site loop S.D.B. Scrofani, J. Chung, J.J.A. Huntley, S. J. Benkovic, P.E. Wright and H.J. Dyson (1999) Biochemistry 38, 14507-14514.

Backbone H^N, N, C^a, C’ and C^b assignments of the 19 kDa DHFR/NADPH complex at 9°C and pH 7.6. E. Zaborowski, J. Chung, G. Kroon, H.J. Dyson and P.E. Wright (2000) J. Biomol. NMR 16, 349-350.

Dynamics of the metallo-b-lactamase from Bacteroides fragilis in the presence and absence of a tight-binding inhibitor. J.J.A. Huntley, S.D.B. Scrofani, M.J. Osborne, P.E. Wright and H.J. Dyson (2000) Biochemistry 39, 13356-13364.

Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism. M.J. Osborne, J. Schnell, S.J. Benkovic, H.J. Dyson and P.E. Wright (2001). Biochemistry 40, 9846-9859.

Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-b-lactamase. J.J.A. Huntley, W. Fast, S.J. Benkovic, P.E. Wright and H.J. Dyson (2003). Protein Sci. 12, 1368-1375.

Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes. M. J. Osborne, R. P. Venkitakrishnan, H. J. Dyson and P. E. Wright (2003). Protein Science 12, 2230-2238.

Effect of co-factor binding and loop conformation on fast methyl dynamics in DHFR. J.R. Schnell H.J. Dyson and P.E. Wright (2004). Biochemistry 43, 374-383.

Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle. R.P. Venkitakrishnan, E. Zaborowski, D. McElheny, S.J. Benkovic, H.J. Dyson and P.E. Wright (2004). Biochemistry 43, 16046-16055.

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis. D. McElheny, J.R. Schnell, J. Lansing, H.J. Dyson and P.E. Wright (2005). Proc. Natl. Acad. Sci. USA 102, 5032-5037.

The dynamic energy landscape of dihydrofolate reductase catalysis. D.D. Boehr, D. McElheny, H. Jane Dyson, P.E. Wright (2006). Science 313, 1638-1642.

Tailoring relaxation dispersion experiments for fast-associating protein complexes. K. Sugase, J.C. Lansing, H.J. Dyson and P.E. Wright (2007). J. Am. Chem. Soc. 129, 13406-13407.

NMR relaxation study of the complex formed between the nuclear coactivator binding domain of CBP and a fragment of the nuclear hormone receptor coactivator ACTR. M.-O. Ebert, S.-H. Bae, H.J. Dyson, P.E. Wright (2008) Biochemistry 47, 1299-1308.