Weikl, T. R.; Hemmateenejad, B.: How conformational changes can affect catalysis, inhibition and drug resistance of enzymes with induced-fit binding mechanism such as the HIV-1 protease. Biochimica et Biophysica Acta: Proteins and Proteomics 1834 (5), pp. 867 - 873 (2013)
Bahrami, A. H.; Lipowsky, R.; Weikl, T. R.: Tubulation and aggregation of spherical nanoparticles adsorbed on vesicles. Physical Review Letters 109 (18), 188102 (2012)
Stieger, T.; Schoen, M.; Weikl, T. R.: Adhesion of surfaces mediated by adsorbed particles: Monte Carlo simulations and a general relationship between adsorption isotherms and effective adhesion energies. Soft Matter 8, pp. 11737 - 11745 (2012)
Weikl, T. R.; Boehr, D. D.: Conformational selection and induced changes along the catalytic cycle of Escherichia coli dihydrofolate reductase. Proteins: Structure, Function, and Bioinformatics 80 (10), pp. 2369 - 2383 (2012)
Krobath, H.; Rózycki, B.; Lipowsky, R.; Weikl, T. R.: Line tension and stability of domains in cell-adhesion zones mediated by long and short receptor-ligand complexes. PLoS One 6 (8), e23284 (2011)
Rózycki, B.; Lipowsky, R.; Weikl, T. R.: Segregation of receptor-ligand complexes in cell adhesion zones: phase diagrams and the role of thermal membrane roughness. New Journal of Physics 12, 095003 (2010)
Noe, F.; Schütte, C.; Vanden-Eijnden, E.; Reich, L.; Weikl, T. R.: Constructing the equilibrium ensemble of folding pathways from short off-equilibrium simulations. Proceedings of the National Academy of Sciences of the United States of America 106 (45), pp. 19011 - 19016 (2009)
Reich, L.; Becker, M.; Seckler, R.; Weikl, T. R.: In vivo folding efficiencies for mutants of the P22 tailspike beta-helix protein correlate with predicted stability changes. Biophysical Chemistry 141 (2-3), pp. 186 - 192 (2009)
Różycki, B.; Lipowsky, R.; Weikl, T. R.: Adhesion of surfaces via particle adsorption: exact results for a lattice of fluid columns. Journal of Statistical Mechanics: Theory and Experiment (11), P11006 (2009)
Weikl, T. R.; Asfaw, M.; Krobath, H.; Rózycki, B.; Lipowsky, R.: Adhesion of membranes via receptor-ligand complexes: domain formation, binding cooperativity, and active processes. Soft Matter 5 (17), pp. 3213 - 3224 (2009)
Weikl, T. R.; Deuster, C. v.: Selected-fit versus induced-fit protein binding: kinetic differences and mutational analysis. Proteins: Structure, Function, and Bioinformatics 75 (1), pp. 104 - 110 (2009)
Weikl, T. R.: Transition states in protein folding kinetics: modeling Phi-Values of small beta-sheet proteins. Biophysical Journal 94 (3), pp. 929 - 937 (2008)
Dill, K. A.; Ozkan, S. B.; Weikl, T. R.; Chodera, J. D.; Voelz, V. A.: The protein folding problem: when will it be solved? Current Opinion in Structural Biology 17 (3), pp. 342 - 346 (2007)
We left the lab coat hanging for a day—but brought our lab equipment with us to meet more than 8,200 visitors. At our 10 stations, we showcased how we learn from nature to develop sustainable solutions—from dye- and pigment-free colors to bio-inspired materials for construction, medicine, and design.
Challenge: It's not just whether a membrane is in a "solid" or "liquid" state that matters—how tightly its molecules are packed also influences how protein-rich droplets (condensates) stick to it Finding: More tightly packed membranes push away condensates, while loosely packed ones attract them Impact: Understanding these interactions is key to grasping essential cellular functions and disease progression
Supported by the EU’s Marie Skłodowska-Curie Actions and the UK Guarantee Scheme, the 'Condensates at Membrane Scaffolds – Integrated Systems as Synthetic Cell Compartments’ doctoral network seeks 17 PhD candidates. This international and interdisciplinary program aims to train future biomedical and biotechnology researchers to explore cellular…
Scientists can now predict structural colors in bacteria. By sequencing a wide range of bacterial DNA and developing an accurate predictive model, reseachers uncovered how bacteria organize themselves into specific patterns within colonies to interfere with light and create iridescence.Their findings hold great promise for sustainable, pigment-free color production.
Imagine switching on a light and being able to understand and control the inner dynamics of a cell. This is what the Dimova group has achieved: by shining lights of different colors on replicates of cells, they altered the interactions between cellular elements. Controlling these complex interactions enables us to deliver specific drugs directly into the cells.
Little is known yet about the interaction between these biomolecular condensate droplets and the membrane-bound organelles. Researchers at the Max Planck Institute of Colloids and Interfaces in Potsdam developed synthetic membraneless organelles and visualized what happens when they meet a membrane.
Prof Silvia Vignolini, Ph.D. is establishing the new Department "Sustainable and Bio-inspired Materials". She is working at the interface of physics, chemistry, biology and materials science and perfectly complements the institute's profile of research on chemistry, materials and sustainability.