We use NMR spectroscopy to assess the structural changes of proteins in response to other molecules in aqueous solution, i.e. under near-physiological condition

label Research theme

About

We work with drug discovery, developing new methods to analyse the structures of protein-ligand complexes in solution by NMR spectroscopy.

We use cell-free protein synthesis as one of our main tools and have leading expertise in the use of unnatural amino acids for site-specific protein modification (for example with tags that allow rapid determination of the binding site, binding orientation and structure of ligand molecules).

Projects

This is one of the big unsolved challenges in biochemistry: how to direct the tag to a single site, ideally inside cells in the presence of other proteins and cell metabolites. The project employs unnatural amino acids for the attachment of fluorophores, EPR tags and NMR tags.

Student intake

Open for Honours, Master, PhD, Summer scholar students

Most proteins and enzymes "live" in solution. Like mechanical machines, their function depends on conformational changes. Using NMR spectroscopy in solution, we develop new methods to determine the movements and conformational changes of proteins, such as the COVID-19 main protease.

Student intake

Open for Honours, Master, PhD, Summer scholar students

Theme

Physical and Biophysical Chemistry

At the ANU, we recently installed world-leading prototype equipment to perform experiments not possible previously with miniscule quantities of material (see picture of sample rotors in comparison with Australian five Cent coin below).

Student intake

Open for Honours, Master, PhD, Summer scholar students

Theme

Physical and Biophysical Chemistry

Members

Leader

ARC Laureate Fellow

Researcher

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Postdoctoral Fellow

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Postdoctoral Fellow

Student

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PhD Candidate

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PhD Candidate

News

Spotlights on Recent JACS Publications has highlighted a JACS paper recently published by Elwy Abdelkader, Haocheng Qianzhu, Yi Jiun Tan, Luke Adams, Thomas Huber and Gottfried Otting (10.1021/jacs.0c11971).

Read the article