Faculty, Graduate Program
NMR is the method of choice in studying unfolded proteins, as well as proteins such as the prion protein that have highly unstructured parts. Since many of the entries in the published genomes appear to code for proteins that should be intrinsically unstructured, an understanding of the nature and behavior of unfolded proteins is assuming increasing importance. Studies with unfolded and partly folded forms of proteins have given us important insights into the earliest steps in the protein folding process. A series of forms of the helical protein apomyoglobin, modeling various stages in the folding process, have now been fully characterized. Using NMR and other spectroscopic techniques, we have been able to map the progressive compaction and increasing structure formation that occurs as the protein folds. A series of mutant proteins has provided important, sometimes surprising, details of the folding process at the level of individual amino acid residues.
B.S., Biochemistry, University of Sydney, 1973
D.Sc., Faculty of Science, University of Sydney, 2009
Ph.D., Inorganic Chemistry, University of Sydney, 1977
1977-1978 Postdoctoral Fellow, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA (supervisor Paul Schimmel).
1979-1984 UNESCO Lecturer, School of Chemistry, University of New South Wales Australia.
1984-1988 Research Associate, Department of Molecular Biology, The Scripps Research Institute.
1988-1992 Assistant Member, Department of Molecular Biology, The Scripps Research Institute.
1992-1997 Associate Professor, Department of Molecular Biology, The Scripps Research Institute.
1997-2001 Associate Professor with Tenure, Department of Molecular Biology, The Scripps Research Institute
2001-Present Professor, Department of Molecular Biology, The Scripps Research Institute
1971 Roslyn Flora Goulston Prize for Biochemistry, Faculty of Science, University of Sydney.
1977-1978 Postdoctoral Award, Damon Runyon-Walter Winchell Cancer Fund.
2009 Awarded D.Sc., Faculty of Science, University of Sydney.
2010 Distinguished Scientist Award, San Diego Section of the American Chemical Society.
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.
Interaction of the IkBa C-terminal PEST sequence with NF-kB: Insights into the inhibition of NF-kB DNA binding by IkBa. S.C. Sue and H.J. Dyson (2009). J. Mol. Biol. 388, 824-838.
Linking folding and binding. P.E. Wright and H.J. Dyson (2009) Curr. Opin. Struct. Biol. 19, 31-38.
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.
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