Andreas's Background and Interests
I studied biochemistry and molecular biology at Friedrich-Schiller-University in Jena, Germany. During my undergraduate years, I was awarded a Fulbright scholarship and moved to the University of Utah for a year abroad. After somehow making it into a Ph.D. program, I stayed for five-and-a-half years in Chris Hill's lab in the Department of Biochemistry. I obtained a Ph.D. in biochemistry for demonstrating a general mechanism for proteasome activation involving a conserved open-gate conformation.
In 2005, I followed a dream and moved to France for my first postdoc. A Marie-Curie-Fellowship made that possible financially. For two-and-a-half years, I worked in Andrea Dessen's lab at the Institut de Biologie Structurale in Grenoble. I was interested in elucidating, at atomic detail, the mechanism of bacterial type III secretion. We got close to crystallizing the secretion pore proteins, but I had to abandon the project in the end because of lack of continued funding.
In the summer of 2007, I gave in to gravity and moved to the center of the universe – London. I am a research associate with Paul and Xiaodong working on a number of projects related to AAA ATPases. Below is a summary of my current activities. If you want to know more, have a look at my C.V.
Endoplasmic reticulum-associated degradation
The process of endoplasmic reticulum-associated degradation (ERAD; for a recent review, see Vembar and Brodsky, 2008) serves to pull unfolded or misfolded proteins from the endoplasmic reticulum before they can aggregate and cause major damage to the cell. The AAA ATPase p97, complexed to an Npl4–Ufd1 dimer, is the major driving force behind retrotranslocation. The nature of the channel has not unambiguously been resolved yet, but it is suspected that Derlin serves that function. Proteins that interact with Derlin and have a role in ERAD are SVIP and the RING finger ubiquitin ligase gp78.
I am working on resolving the structures of the various players in ERAD. This is a collaborative effort with Prof. Steve Matthews and entails crystallization, NMR and electron microscopy. Some of the results of this work have recently been published PNAS (Bebeacua et al., 2012).
X-ray crystallography
I am currently involved in a number of crystallographic projects at various stages between crystallization and refinment whose nature will remain shrouded in mystery until the big splash. Furthermore, I apply my knowledge and experience in crystallography to various unsolved problems, trying to extricate useful information from datasets with pseudosymmetry, lattice translation, twinning. If you have a perplexing dataset yourself, why not come over and have a chat?
1.2Å data obtained at Diamond.
Molecular modeling and dynamics
Over the last few years, I've starting using advanced molecular modeling and molecular dynamics tools like Rosetta and NAMD to give a theoretical backing to biological or biochemical observations that collaborators have obtained. Specifically, I've studied the hetero-dimerization potential of nucleosome assembly proteins (Attia et al., 2011) and the effect of phosphorylation on a MAP kinase.
Effect of phosphorylation on the structure of MEK1.
IT support
I wrote the webpage you are reading. I have also implemented a plasmid database and a wiki, two structures that help the lab be organized and more efficient in its research efforts. Whenever there are general problems with linux workstations or Windows XP and OSX computers, I try to help.
Writing
In my spare time, I write – sometimes more, sometimes less. The output of my creativity can be admired at my blog and my homepage.