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 loopS.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 HN, N, Ca, C and Cb 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.
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,
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.
Transfer of flexibility between ankyrin repeats in IkBa upon formation of the NF-kB complex. S.-C. Sue, C. Cervantes, E.A. Komives and H.J. Dyson (2008) J. Mol. Biol. 380, 917-931.
Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis. D.D. Boehr, H.J. Dyson and P.E. Wright (2008) Biochemistry 47, 9227-9233.
Mapping protein folding landscapes by NMR relaxation.
P.E. Wright, D.J. Felitsky, K. Sugase and H.J. Dyson (2009). In Water and Biomolecules Physical
Chemistry of Life Phenomena (K. Kuwajima, F. Hirata, Y. Goto, M. Kataoka and M. Terazima,
eds)
Interaction of the IκBα C-terminal
Prediction of the rotational tumbling for proteins with long disordered segments. S.H. Bae, P.E. Wright and H.J. Dyson (2009) J. Am. Chem. Soc. 131, 6814-6821.
Functional dynamics of the folded ankyrin repeats of IkBa revealed by nuclear magnetic resonance C.F. Cervantes, P.R.L. Markwick, S.-C. Sue, J.A. McCammon, H.J. Dyson and E.A. Komives (2009). Biochemistry 48, 8023-8031.
Millisecond timescale fluctuations in dihydrofolate reductase are
exquisitely sensitive to the bound ligands. D.D. Boehr, D. McElheny, H.J. Dyson and P.E. Wright (2010) Proc. Natl. Acad. Sci. USA 107,
1373-1378.
A dynamic knockout reveals that conformational fluctuations influence the chemical step of catalysis. G. Bhabha, J. Lee, D.C. Ekiert, J. Gam, I.A. Wilson, H.J. Dyson, S.J. Benkovic and P.E. Wright (2011) Science 332, 234-238.
The RelA nuclear localization signal folds upon binding to IkBa. C.F. Cervantes, S. Bergqvist, M. Kjaergaard, G. Kroon, S.-C. Sue, H.J. Dyson and E.A. Komives (2011) J. Mol. Biol. 405, 754-764.
Detection of a ternary complex of NFkB and IkBa with DNA provides insights into how IkBa removes NFkB from transcription
sites. S.C. Sue, V. Alverdi, E.A. Komives and H.J. Dyson (2011) Proc. Natl. Acad. Sci. USA 108, 1367-1372.
Role of disorder in IkB-NFkB interaction. H.J. Dyson and E.A. Komives (2012) IUBMB Life (in press)