- Aug 12, 2017
- Active Faculty
Condensed Matter Physics - Experimental
Biomedical-Physical Sciences Bldg.
567 Wilson Rd., Room 4227
B140 Biomedical-Physical Sciences Bldg.
B175 Biomedical-Physical Sciences Bldg.
B. Ahmad, L.J. Lapidus, Curcumin Prevents α-synuclein Aggregation by Controlling Intramolecular Diffusion, Journal of Biological Chemistry 287(12): pp. 9193-9199 (2012).
B. Ahmad, Y. Chen, L.J. Lapidus, Aggregation of α-synuclein is Kinetically Controlled by Intramolecular Diffusion, Proceedings of the National Academy of Sciences. 109(7): pp. 2336-2341 (2012).
Y. Chen, W.J. Wedemeyer, L.J. Lapidus, A General Model of Unfolded Proteins under Folding Conditions. J. Phys. Chem. B. 114, 15969-15975 (2010).
S. A. Waldauer, O. Bakajin, L.J. Lapidus, Extremely Slow Intramolecular Diffusion in Unfolded Protein L, Proceedings of the National Academy of Sciences 107, 13713-13717 (2010).
V.A. Voelz, V.R. Singh, W.J. Wedemeyer, L.J. Lapidus, V.S. Pande, Unfolded state dynamics and structure of protein L characterized by simulation and experiment. Journal of the American Chemical Society, 132, 4702-4709 (2010).
Y. Chen, C. Parrini, N. Taddei, L.J. Lapidus, Conformational Properties of Unfolded HypF-N, J. Phys. Chem. B 113, 16209-16213 (2009).
S. DeCamp, S.A. Waldauer, A. Naganathan, O. Bakajin, L.J. Lapidus, Direct Observation of Downhill folding of l-repressor in a Microfluidic Mixer, Biophys. J. 97, 1772-1777 (2009).
Professional Activities & Interests / Biographical Information
Biological Physics, Protein Folding
The Lapidus lab studies protein folding using optical spectroscopy and microfluidics. We currently have the fastest continuous flow mixer in the world, which can mix two solutions and prompt protein folding in ~4 microseconds. We are currently developing new mixers to improve mixing time and apply microfluidics to new spectroscopic methods.
The Lapidus lab also studies the early stages of folding and the dynamics of unfolded proteins. We recently showed that intramolecular diffusion of unfolded protein L is 1000 times slower than previously estimated. This finding may profoundly change the way protein folding theories are constructed because the search for native structure may be limited by this slow reconfiguration. We are also looking at how the rates of intramolecular diffusion depends on sequence and have found that this rate is related to the propensity for a protein to aggregate.
Protein aggregation has effects in biological systems (for example, in plaque formation found in several human maladies such as Parkinson's disease and Alzheimer's). We wish to understand the folding processes at a fundamental level, to determine the differences between ordinarily functioning proteins and those which have clumped together to form plaques. A better understanding of the processes may lead eventually to treatments or preventive techniques for these and other diseases.
For further information on some early results of this research, see the following "MSU Today" articles: “Researchers Identify Path to Treat Parkinson's Disease at Inception” (26 January 2012) and “Curcumin Shows Promise in Attacking Parkinson's Disease” (20 March 2012).