

Confirmed speakers:
Assoc. Prof. Ashley Buckle Monash University
Title: Conformational plasticity in alpha-1 antitrypsin:
the role of dynamics in serpin misfolding, aggregation and disease.
Ashley Buckle is an NHMRC Senior Research Fellow in the Department of Biochemistry and Molecular Biology at
Monash University, Australia. He completed his PhD in 1994 in the laboratory of Prof Sir Alan Fersht at the University of
Cambridge, undertaking research on the structure determination of protein- DNA and protein-protein complexes. As a
postdoctoral then staff scientist at the MRC Centre Cambridge, he made contributions to the understanding of protein
stability, molecular recognition and the action of molecular chaperones. At Monash since 2003, his research is aimed at
understanding how the structure and dynamics of proteins dictates their function. His lab uses a multidisciplinary
approach including protein crystallography, bioinformatics, software development, and molecular simulation.
Prof. Nick Dixon University of Wollongong
Title: Protein-protein interactions in the bacterial
replisome
Nick Dixon holds a PhD in Biochemistry from the University of Queensland. He was a Research Fellow in Chemistry at
ANU, before being awarded a C.J. Martin and Fulbright Fellowships to study E. coli DNA replication with Arthur Kornberg
at Stanford. He returned to the ANU as a Queen Elizabeth II Fellow in 1983, and was appointed to the staff of the
Research School of Chemistry, ANU in 1986. He left ANU in 2006 to take up his present position as Professor of
Biological Chemistry at the University of Wollongong. He is currently an ARC Australian Professorial Fellow.
Assoc. Prof. Julian Eaton-Rye Otago University
Title: Auxiliary proteins of photosystem II: tuning the enzyme for optimal activity
Associate Professor Julian Eaton-Rye completed a BSc Honors degree in Botany from the University of Manchester, UK in 1981 and obtained his
PhD (Plant Physiology) in 1987 at the University of Illinois at Urbana-Champaign. After postdoctoral research at the National Institute of
Basic Biology, Okazaki, Japan, Arizona State University, and Brookhaven National Laboratory, USA, he moved to Otago University in 1994.
Throughout his career he has concentrated on the biogenesis, structure and function of photosystem II: the light-driven water-splitting
enzyme of photosynthesis. Many studies in his laboratory have utilised the cyanobacterium Synechocystis sp. PCC 6803 as a model
organism and combine physiological, biochemical and molecular genetic approaches to understanding the molecular details of how the
protein framework of the photosystem supports the sustained oxygen-evolving activity of this enzyme across a wide range of environmental
conditions. Currently the lab is concentrating on the roles of a number of polypetide subunits that are essential in the "life-cycle" of this
enzyme but are not present in the X-ray-derived structures obtained for the mature complex.
Dr Mike Griffin University of Melbourne
Title: Methionine oxidation induces amyloid fibril formation by apolipoprotein A-I.
Prof. Michael Hecht Princeton University, US
Title: TBA
Research in the Hecht group is focused in two areas: Synthetic Biology: From Protein Design to Artificial Genomes and
Alzheimer’s Disease: Molecular Underpinnings and the Search for Novel Therapeutics.
Assoc. Prof. Andy Hill University of Melbourne
Title: Intercellular trafficking of proteins and
RNA in neurodegenerative diseases.
Associate Professor Andrew Hill is a Principal Research Fellow in the Department of Biochemistry and Molecular
Biology at the University of Melbourne. His laboratory studies the molecular and cellular biology of neurodegenerative
disorders such as Alzheimer's and prion diseases. In 1992, he began working on prion diseases in the UK, researched
the molecular properties of human and animal prion strains, and identified the link between BSE and a new form of prion
disease in humans - variant Creutzfeldt-Jakob disease that emerged in 1996. This work led to a number of high profile
publications in Nature and Science and to the development of a diagnostic and classification system for human prion
diseases. Andrew first came to Australia in 2000 as a Wellcome Trust Travelling Prize Research Fellow where he
expanded his research interests into other neurodegenerative disorders such as Alzheimer's and Parkinson's
diseases. Andrew's research team uses in vitro and in vivo models to look at how abnormal prion proteins travel from
cell to cell and factors that affect prion infection. This work has extended into identifying similar pathways involved in the
processing of the amyloid precursor protein (APP) involved in Alzheimer's disease. His laboratory also works on the
basic biology of the prion protein and APP to understand their role in the disease process in more detail, with the goal of
translating this into the design of novel therapeutics and diagnostics.
Assoc. Prof. Craig Hutton University of Melbourne
Title: Solid phase synthesis of covalently
cross-linked peptides: application to the study of dityrosine-linked A-beta dimers
Craig Hutton obtained his undergraduate and PhD degrees from the University of Adelaide before completing
postdoctoral studies at the University of California, Berkeley and The University of Melbourne (Australian Postdoctoral Research Fellow).
He was then appointed to the School of Chemistry at The University of Sydney, before returning to The University of Melbourne in 2003,
where he is now Associate Professor. His research interests include the study of dityrosine cross-linked peptides and proteins, the
synthesis of biologically active cyclic peptide natural products and the enzymology of the lysine biosynthetic pathway.
Prof. Bostjan Kobe University of Queensland
Title: Using structural information to predict
peptide-protein interactions: application to protein kinases, MHC class II and nuclear localisation
Bostjan Kobe is the ARC Federation Fellow at the School of Chemistry and Molecular Biosciences, the University of
Queensland (UQ). Bostjan Kobe received his BSc (Hons) from the Univeristy of Ljubljana, Slovenia, and his PhD from
the University of Texas Soutwestern Medical Center at Dallas, USA, under the supervision of Johann Deisenhofer. He
worked as Postdoctoral Fellow at Howard Hughes Medical Institute in Dallas Texas, and at St Vincent's Institute of
Medical Research in Melbourne, Australia. He has been at the University of Queensland since the year 2000. He has
been awarded the Minister's Prize for achievement in Life Sciences in 2001. His laboratory focuses on the role of protein
structure and interactions in the molecular and cellular functions of these molecules.
Prof. Kurt Krause University of Otago
Title: Orf virus chemokine binding protein maintains tight binding across
chemokine families
Kurt Krause is a structural biologist and a clinical specialist in infectious diseases with a particular interest in the pathogenicity
of infectious agents such as streptococci, mycobacteria and the HIV virus. In 1980 he completed an M. D. with honours from
Baylor College of Medicine and then earned his MA and PhD at Harvard University in the laboratory of Professor William N. Lipscomb, Jr.
Following a short period of postdoctoral work, also at Harvard, he completed fellowships in Internal Medicine and Infectious
Diseases at Baylor Affiliated Hospitals in Houston, Texas. He served on the academic faculty of the University of Houston and
Baylor College of Medicine and on the medical attending staff of Ben Taub General Hospital, The Methodist Hospital and St. Luke's
Hospital before moving to New Zealand in 2006. He is currently the Head of the Department of Biochemistry and the Director of the
Webster Centre for Infectious Diseases at the University of Otago in Dunedin, New Zealand. He is a member of the American
Academy for the Advancement of Science, the American Chemical Society, the American Crystallography Association, and is a
Fellow in the Infectious Diseases Society of America.
Prof Tom Laue University of New Hampshire, US
Title: Proximity energy framework for
biochemistry
Tom Laue is the Capenter Professor of Molecular, Cellular and Biomedical Sciences, and professor of Material
Sciences at the University of New Hampshire. He is the Director of both the Center to Advance Molecular Interaction
Science and the Biomolecular Interaction Technologies Center.
He received his bachelor's degree in Natural Sciences from the Johns Hopkins University in 1971and his Ph.D. in
Biophysics and Biochemistry from the University of Connecticut in 1981. His post-doctoral studies were conducted at the
University of Oklahoma. Between 1969 and 1975, he worked as a technician in the deep space program of NASA.
He joined the University of New Hampshire in 1984 as an Assistant Professor, and teaches both undergraduate and
graduate courses in biochemistry and biophysics. His research focuses on the development of instrumentation and
methods that use the fundamental properties of mass and charge for examining macromolecular interactions. His
instruments can provide unique insights into these interactions, which has resulted in extensive collaborations with both
academic and industrial labs. Tom has over 120 publications, serves on several editorial boards, and gives over one
hundred lectures, seminars and workshops a year.
Dr Sheena McGowan Monash University
Title: Structural basis for the inhibition of the essential Plasmodium falciparum aminopeptidases.
Prof David Millar Department of Molecular Biology, The Scripps Research Institute, US
Title:
Nucleic Acid -- Protein Interactions at the Single-Molecule Level
David Millar received a B. Sc. (Hons) degree from the University of Melbourne and a Ph. D. degree from the California
Institute of Technology, both in Chemistry. After postdoctoral work at Columbia University, he returned to Australia as a
Queen Elizabeth II Fellow in the Department of Chemistry at the University of Sydney. In 1987, he was recruited to the
Scripps Research Institute in La Jolla, California, where he is now Professor in the Department of Molecular Biology.
Throughout his career, Dr. Millar has applied state-of-the-art fluorescence spectroscopic techniques to a range of
biochemical systems. Early studies employed fast time-resolved fluorescence methods to probe the conformational
dynamics of nucleic acids and nucleic acid-protein complexes, including DNA Holliday junctions, the hairpin ribozyme
and DNA polymerases. In recent years, the Millar group has developed a range of single-molecule fluorescence
methods, including both TIRF-based and confocal formats, for the analysis of RNA folding, ribonucleoprotein
assembly and DNA-protein interactions. Current research interests include the analysis of RNA-protein interactions
involved in trafficking of HIV messenger RNA, the assembly pathway of the signal recognition particle, and visualization
of DNA polymerase activity at the single-molecule level.
Dr James Murphy WEHI
itle: Molecular characterization of the haematopoietic
pseudokinase-domain containing proteins, Jak2 and Mlkl
Dr Wayne Patrick Massey University
Title: Promiscuous biomolecular interactions in protein evolution
Wayne Patrick is a senior lecturer in biochemistry at the Institute of Natural Sciences, Massey University (Albany). After completing
a PhD at the University of Cambridge (UK) and a post-doc at Emory University (USA), he returned home to New Zealand in 2007.
Since then, he has mainly just been sitting in his office, while his talented students have done loads of cool experiments to address
questions in protein evolution and engineering.
Dr Chris Squire University of Auckland
Title: Hijacking Ubiquitination: orf, structure prediction, and the SCF ubiquitin ligase complex
Dr. Squire graduated PhD(Chemistry) from Auckland University in 1998 before postdoctoral work with Eddie Arnold (Rutgers) and
Ted Baker (Auckland). He has been a member of the UoA faculty since 2007. Chris applies X-ray crystallography and molecular
modeling in Drug Discovery (cancer, antibacterial, alzheimers) and in studying poxvirus immune evasion and entry-fusion mechanisms.
Dr Céline Valéry, BIC, University of Canterbury
Title: Functional peptide assemblies: structural features and biomimetic applications
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