Edward Lemke
Edward Lemke studied Chemistry since 1997 with a focus on Physical Chemistry at the Technical University of Berlin, where he received his Diploma in 2001. He gained further biochemistry expertise during a stay at the University of Oklahoma where he also received a Master of Science in the same year. He then moved to the Max Planck Institute for Biophysical Chemistry to join the Department of Membrane Biophysics. As a fellow of the Boehringer Ingelheim foundation he studied the real-time dynamics of synaptic vesicles within small living hippocampal boutons using advanced fluorescence microscopy and correlation spectroscopy approaches. In 2005 he moved to the Scripps Research Institute where he was working as a joint postdoc in the group of Prof. Peter Schultz and Prof. Ashok Deniz. In Peter Schultz’s department he developed novel chemical biology tools that allow photocontrol of protein phosphorylation noninvasively within living cells. As part of a collaboration with the Deniz lab, he also worked on strategies to manipulate proteins with small fluorescent dyes for subsequent single molecule studies. In the Deniz lab, he furthermore combined single molecule with microfluidic approaches to enhance biological single molecule measurements. Moreover, he contributed to single molecule protein folding studies of intrinsically disordered and amyloid forming proteins. Since 2009 Edward Lemke is leading an independent research group at the EMBL in Heidelberg. His group is located in the Structural and Computational Biology Unit, but is also associated with the Cell Biology and Biophysics group. The main interests of his group are the application of single molecule techniques to study highly dynamic and complex biomolecular machineries.
http://www.embl.de/research/units/scb/lemke/index.html
Single Molecule, Microfluidic and Genetically Encoded Tools to Study Protein Structure and Dynamics
In any complex biological system, a mosaic of molecular states and reaction pathways exist in parallel, which often cannot be revealed by conventional “ensemble” techniques. A powerful approach is direct observation of biomolecular mechanisms at the single molecule level, which probes the distribution of behaviors rather than just the average1. However, the strength of single molecule techniques to monitor protein structure and function is largely hampered by several complications such as the requirement for site-specific labeling, dye stability and even seemingly simple things as non-specific sticking of proteins to surfaces. I will present how genetically encoding unnatural amino acids can overcome the labeling bottleneck by serving as biocompatible chemical handles 2. Furthermore, I will show how a microfluidic device with built-in “rapid gas exchange technology” can address photo-stability as well as non-specific sample adhesion issues3. En route with describing these tools the relevance of single molecule studies for biology will be highlighted by presenting data that allows for a better understanding of a-synuclein structure and dynamics, a protein linked to Parkinson and Alzheimer diseases 4.
(1) Deniz, A. A.; Mukhopadhyay, S.; Lemke, E. A. J R Soc Interface 2008, 5, 15-45.
(2) Brustad, E. M.; Lemke, E. A.; Schultz, P. G.; Deniz, A. A. J Am Chem Soc 2008, 130, 17664-5.
(3) Lemke, E. A.; Gambin, Y.; Vandelinder, V.; Brustad, E. M.; Liu, H. W.; Schultz, P. G.; Groisman, A.; Deniz, A. A. J Am Chem Soc 2009, 131, 13610-2.
(4) Ferreon, A. C.; Gambin, Y.; Lemke, E. A.; Deniz, A. A. Proc Natl Acad Sci U S A 2009, 106, 5645-50.
