My main expertise is the characterisation of proteins in vitro and in silico. I am happy to look into any proteins you might be interested studying this way, please do not hesitate to contact matthias.fellner@otago.ac.nz
For in vitro studies I have set up a pipeline for cloning, expressing and purifying any given protein using an Escherichia coli system that might be of interest to collaborators. Many factors influence if E. coli can produce high quality protein for in vitro studies. Having produced a wide range of proteins from different organisms, of various lengths and types I am now in a position to estimate ahead of starting a project the chances of success. I am experienced in optimising the construct to be inserted into the production E. coli vector, including truncations, domain separations and fusion to other proteins. In addition, the purification protocol can be optimised based on my knowledge to improve protein production, including purification of insoluble protein from E. coli inclusion bodies. I also have used other production systems like Lactococcus lactis and can connect to other local researchers who routinely produce proteins from Mycobacterium smegmatis, yeast, insect cells, human cells or natural sources.
Once purified protein is produced I am an expert in determining their structure/function relationship:
- Characterisation of protein/enzyme functions using site directed mutagenesis, mass spectroscopy, nuclear magnetic resonance, UV/Vis, Fluorescence spectroscopy, HPLC/FPLC, enzyme coupled assays, chemical crosslinking, chemical synthesis and assay components.
- Characterisation of structures using X-ray crystallography, electron microscopy, circular dichroism and Multiangle light scattering with over 50 currently deposited entries in the protein databank (PDB). Protein databank: Fellner, M.
X-ray crystallography is my main tool for structure determination. I welcome collaboration on any project where purified protein is already available to attempt to grow protein crystals. I am in charge of access to the Australian synchrotron protein crystallography beamlines for Otago researchers and can be involved in every step from optimal purification for crystallisation, to setting up crystal drops, shipping crystals to the synchrotron and measure remotely or in person. If crystallisation conditions are available in the literature for a protein, I can help to determine ligand bound structures. Nearly every structure I have determined in the past contains a ligand from metals to drugs. In any given year I measure 500+ crystals at the synchrotron spanning a variety of proteins and I am always looking to add more targets.
In silico studies ahead of protein production can be used for prediction of structure and function. I am happy to analyse any given protein sequence of a potential collaborator. These gives a quick overview of what is already know in function and structure databases.
Once a structure is determined I have experience using a structure for a wide range of in silico tools like molecular dynamics, ligand docking and structure homolog searches.
Please email matthias.fellner@otago.ac.nz if you have any questions. I am happy to look at any protein sequence for you. At the moment all costs of a preliminary experiment associated with the methods described above from cloning to measurement of protein crystals would be covered by myself. I am especially interested to build on any successful produced protein into co-supervised student projects and joint funding applications.
