The research in my group is directed towards biophysics with an emphasis on biophysical fluorescence. This highly interdisciplinary domain requires the interaction of chemists, physicists, and biologists. Only a concerted effort of these three groups will allow us to tackle the problems in the life sciences. The close proximity of departments of biology, biochemistry, chemistry, and physics at the National University of Singapore on one side and the research institutes (RIs) on the other side, allows us to develop physical and chemical methods for the study of biological questions on one hand and to apply these methods to the frontier in biology on the other hand. Our interests lie accordingly in the different areas that interact freely to advance this research field.
Construction and development of new optical tools.
Optical Spectroscopy is one of the most sensitive tools available in the life sciences. Proteins can be studied not only in ensembles but as well on the single molecule level. Besides using well established methods in our group (e.g. Fluorescence Correlation Spectroscopy, Fluorescence Resonance Energy Transfer), we also plan to develop new spectroscopy and microscopy tools and new mathematical procedures to study proteins on a single molecule level in vitro and in vivo.
Study of selected proteins and protein complexes on a single molecule level and in living cells.
In collaboration with the Department of Biological Sciences, the Department of Microbiology and the RIs we will study the properties of selected proteins and peptides to elucidate their function on a molecular level. At the moment we concentrate on either antimicrobial peptides and their interaction with bacterial membranes, or on the study of transmembrane proteins (G-protein coupled receptors, growth factors) and their structure, function and interactions.
One of the most interesting questions in biology is the relationship between the structure and function of proteins. With the fluorescence tools developed in our group we hope to shed some light on this question by in vitro experiments. In a complementary approach we will study the proteins in living cells because proteins are in many cases very sensitive to their environment and only when studied under physiological conditions can we determine their exact function.
Krieger, J.W; Singh, A.P; Bag, N; Garbe, C.S; Saunders, T.E; Langowski, J; Wohland, T. Imaging fluorescence (cross-) correlation spectroscopy in live cells and organisms. Nat Protoc. 2015 Dec;10(12):1948-74.
Bag, N; Huang, S; Wohland, T. Plasma Membrane Organization of Epidermal Growth Factor Receptor in Resting and Ligand-Bound States. Biophys J. 2015 Nov 3;109(9):1925-36.
Eshaghi, M; Sun, G; Grüter, A; Lim, C.L; Chee, Y.C; Jung, G; Jauch, R; Wohland, T; Chen, S. L. Rational Structure-Based Design of Bright GFP-Based Complexes with Tunable Dimerization. Angew Chem Int Ed Engl. 2015 Oct 8. doi: 10.1002/anie.201506686. [Epub ahead of print]
Teh C, Sun G, Shen H, Korzh V, Wohland T. Modulating expression level of secreted Wnt3 influences cerebellum development in zebrafish transgenics. Development. 2015 Nov 1;142(21):3721-33
Mistri, T.K.; Devasia, A.G.; Chu, L.T.; Ng, W.P.; Halbritter, F.; Colby, D.; Martynoga, B.; Tomlinson, S.R.; Chambers, I.; Robson, P.; Wohland, T. Selective influence of Sox2 on POU transcription factor binding in embryonic and neural stem cells, EMBO Rep 2015 Aug 11. pii: e201540467
Ng, X.W.; Bag, N.; Wohland, T. Characterization of Lipid and Cell Membrane Organization by the Fluorescence Correlation Spectroscopy Diffusion Law, CHIMIA International Journal for Chemistry 69 (3), 112-119.
Rashid, R.; Chee, S.M.L.; Raghunath, M.; Wohland, T. Macromolecular Crowding Gives Rise to Microviscosity, Anomalous Diffusion & Accelerated Actin Polymerization, Physical Biology (2015) Apr 30; 12(3): 034001
Sun, G.; Guo, S.M.; Teh, .; Korzh, V,; Bathe, M.; Wohland, T. Bayesian Model Selection Applied to the Analysis of FCS Data of Fluorescent Proteins in vitro and in vivo, Analytical chemistry (2015) Apr 21; 87(8): 4326-33
Rashid, R.; Beyer, S.; Blocki, A.; Le Visage, C.; Trau, D.; Wohland, T.; Raghunath, M. Mitochondrial Routing of Glucose and Sucrose Polymers After Pinocytotic Uptake: Avenues For Drug Delivery, Biomacromolecules (2014) Jun 9;15(6):2119-27
Rashid, R.; Lim, N.S.J.; Chee, S.M.L.; Png, S.N.; Wohland, T.; Raghunath, M. Novel Use for Polyvinylpyrrolidone as a Macromolecular Crowder for Enhanced Extracellular Matrix Deposition and Cell Proliferation, Tissue Engineering Part C Methods (2014) Dec; 20(12):994-1002
Machan, R.; Wohland, T. Recent Applications of Fluorescence Correlation Spectroscopy in Live Systems, FEBS Letters 588 (2014) 3571–3584.
Singh, A.P.; Wohland, T. Applications of imaging fluorescence correlation spectroscopy, Curr. Op. Chem. Biol. (2014) 20:29-35.
Guo, S.M.; Bag, N.; Mishra, A.;Wohland, T.; Bathe, M. Bayesian Total Internal Reflection Fluorescence Correlation Spectroscopy Reveals hIAPP-Induced Plasma Membrane Domain Organization in Live Cells, Biophy. J. 106 (2014) 190–200
Bag, N.; Yap, D.H.X.; Wohland, T. Temperature dependence of diffusion in model and live cell membranes characterized by imaging fluorescence correlation spectroscopy, BBA Biomembranes 1838 (2014) 802–813.
Krieger, J.W.; Singh, A.P.; Garbe, C.S.; Wohland, T.; Langowski, J. Dual-Color Fluorescence Cross-Correlation Spectroscopy on a Single Plane Illumination Microscope (SPIM-FCCS), Optics Express 22(3) (2014) 2358-2375. Supplementary material
Bag, N.; Wohland, T. Imaging Fluorescence Fluctuation Spectroscopy: New Tools for Quantitative Bioimaging. Annu. Rev. Phys. Chem. 65 (2014) 225–48.