The Risselada group employs molecular simulation techniques to tackle relevant problems in the field of biophysics and related molecular fields within a multidisciplinary and interdisciplinary research environment (e.g., the Resolv excellence cluster). Particularly, we focus on the development of enhanced sampling and multiscale methods to study phenomena occurring at fluid (e.g., biological lipid membranes) and solid interfaces (e.g., metal interfaces and graphene). An important current focuses is on a subject coined "facial recognition of fluid interfaces", i.e., how can (bio)molecules optimally recognize and bind fluid interfaces despite their highly disordered and dynamic nature. To this aim, we develop evolutionary molecular dynamics simulations (evo-MD) methods which couple evolutionary algorithms (sampling of chemical space) to coarse-grained molecular dynamic simulations (sampling of phase-space) to resolve the global optima in chemical space. In essence, evo-MD enables molecules to adapt themselves to optimally recognize fluid interfaces in the course of a simulated evolution. Our research may yield unique insights on how biomolecules such as peptides and proteins recognize distinct fluid features in biological lipid membranes with interesting applications for the fields of drug design, surfactant design, and the design of (bio)sensors.
- E.M. Blokhuis, M. D'Agostino, A. Mayer, H.J. Risselada
Fusion pores live on the edge
J. Chem. Phys. Lett., 11(4):1204–1208, 2020
- Y.G. Smirnova, H.J. Risselada, M. Müller
Thermodynamically reversible paths of the first fusion intermediate reveal an important role for membrane anchors of fusion proteins
PNAS 116(7): 2571-2576, 2019
- M. D'Agostino, H. J. Risselada, A. Lürick, C. Ungermann, and A. Mayer
A tethering complex drives the terminal stage of SNARE-dependent membrane fusion
Nature, 551: 634-638, 2017
- M. D'Agostino, H.J. Risselada, A. Mayer
Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition
EMBO reports, 17(11):1590-1608, 2016
- H.J. Risselada
Simulations Move Toward a Cure for Viral Diseases
Structure, 23(3):439-440, 2015
- H.J. Risselada, Y. Smirnova, H. Grubmüller
Free energy landscape of rim-pore expansion in membrane fusion
Biophys. J., 107: 2287-2295, 2014
- H.J. Risselada, G. Bubnis, H. Grubmüller
Expansion of the fusion stalk and its implication for biological membrane fusion
Proc. Natl. Acad. Sci. USA., 111:11043-110487, 2014
- H.J. Risselada
Membrane fusion stalks and 'lipid rafts': A love-hate Relationship
Biophysical J. (Letter), 112(12): 2475-2478, 2017
- D. Milovanovic, A. Honigmann,..., H.J. Risselada, ..., S.W. Hell, G. Van den Bogaart, R. Jahn
Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains
Nature communications, 6:5984, 2015
- T. Fischer, H.J. Risselada, R.L.C Vink
Membrane lateral structure: The influence of immobilized particles on domain size
Phys. Chem. Chem. Phys., 14:14500-14508, 2012
- G. Van den Bogaart, K. Meyenberg K, H.J. Risselada, H. Amin, K.I. Willig, B.E. Hubrich, M. Dier, S.W. Hell, H. Grubmüller, U. Diederichsen, R. Jahn
Membrane protein sequestering by ionic protein-lipid Interactions
Nature, 479:552-55, 2011
- H.J. Risselada, S.J. Marrink, M. Müller
Curvature-dependent elastic properties of liquid-ordered domains result in inverted domain sorting on uni-axially compressed vesicles
Phys. Rev. Lett., 106: 148102, 2011
- L.A. Belyaeva, L. Jiang, A. Soleimani, J. Methorst, H.J. Risselada, G.F. Schneider
Liquids relax and unify strain in graphene
Nat. Comm. 11(898), 2020
- A. Gladytz, B. Abel, H.J. Risselada
Gold-Induced Fibril Growth:The Mechanism of Surface-Facilitated Amyloid Aggregation
Angew. Chem. Int. Ed. 55:12242-46, 2016
- Laura J. Endter, H.J. Risselada
Where are those lipidic nano rings?
J. Colloid Interface Sci., 587:789-796, 2020
- Laura J. Endter, Y.G.Smirnova, H.J. Risselada
Density Field Thermodynamic Integration (DFTI): A ’soft’ approach to calculate the free energy of surfactant self-assemblies
J. Phys. Chem. B, 124(31):6775–6785, 2020
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Location & approach
The campus of TU Dortmund University is located close to interstate junction Dortmund West, where the Sauerlandlinie A 45 (Frankfurt-Dortmund) crosses the Ruhrschnellweg B 1 / A 40. The best interstate exit to take from A 45 is “Dortmund-Eichlinghofen” (closer to South Campus), and from B 1 / A 40 “Dortmund-Dorstfeld” (closer to North Campus). Signs for the university are located at both exits. Also, there is a new exit before you pass over the B 1-bridge leading into Dortmund.
To get from North Campus to South Campus by car, there is the connection via Vogelpothsweg/Baroper Straße. We recommend you leave your car on one of the parking lots at North Campus and use the H-Bahn (suspended monorail system), which conveniently connects the two campuses.
TU Dortmund University has its own train station (“Dortmund Universität”). From there, suburban trains (S-Bahn) leave for Dortmund main station (“Dortmund Hauptbahnhof”) and Düsseldorf main station via the “Düsseldorf Airport Train Station” (take S-Bahn number 1, which leaves every 20 or 30 minutes). The university is easily reached from Bochum, Essen, Mülheim an der Ruhr and Duisburg.
You can also take the bus or subway train from Dortmund city to the university: From Dortmund main station, you can take any train bound for the Station “Stadtgarten”, usually lines U41, U45, U 47 and U49. At “Stadtgarten” you switch trains and get on line U42 towards “Hombruch”. Look out for the Station “An der Palmweide”. From the bus stop just across the road, busses bound for TU Dortmund University leave every ten minutes (445, 447 and 462). Another option is to take the subway routes U41, U45, U47 and U49 from Dortmund main station to the stop “Dortmund Kampstraße”. From there, take U43 or U44 to the stop “Dortmund Wittener Straße”. Switch to bus line 447 and get off at “Dortmund Universität S”.
The AirportExpress is a fast and convenient means of transport from Dortmund Airport (DTM) to Dortmund Central Station, taking you there in little more than 20 minutes. From Dortmund Central Station, you can continue to the university campus by interurban railway (S-Bahn). A larger range of international flight connections is offered at Düsseldorf Airport (DUS), which is about 60 kilometres away and can be directly reached by S-Bahn from the university station.
The H-Bahn is one of the hallmarks of TU Dortmund University. There are two stations on North Campus. One (“Dortmund Universität S”) is directly located at the suburban train stop, which connects the university directly with the city of Dortmund and the rest of the Ruhr Area. Also from this station, there are connections to the “Technologiepark” and (via South Campus) Eichlinghofen. The other station is located at the dining hall at North Campus and offers a direct connection to South Campus every five minutes.
The facilities of TU Dortmund University are spread over two campuses, the larger Campus North and the smaller Campus South. Additionally, some areas of the university are located in the adjacent “Technologiepark”.