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- Delft University of Technology (TU Delft); Published yesterday
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- Delft University of Technology (TU Delft); 16 Oct ’25 published
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Field
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biomedical engineers that collaborate in a close-knit team. The lab hosts a range of state-of-the-art single-molecule microscopes in optical laboratories, as well as wet-chemical labs for sample preparation
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Protein lipidation is the covalent attachment of lipids to proteins, regulating their trafficking, protein–protein interactions, and stability. This post-translational modification is dynamically
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dynamics of Earth’s systems from the mountains to the sea, and the interaction in between. This knowledge is essential for the sustainable management of our planet and to guarantee the availability
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adapt to environmental change, including ecological and evolutionary effects on species interactions, behaviour and community composition. We make innovative contributions to the fundamental research
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by a EU programme Is the Job related to staff position within a Research Infrastructure? No Offer Description * Four-year fully funded projects with possible extension and state-of-the-art facilities
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research projects that contribute to the goals of this PhD project. We offer a stimulating and interactive research environment, free use of all state-of-the-art facilities, a competitive salary. We offer a
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The project focuses on the experimental realization and study of artificial microswimmers/microrobots that can move and interact autonomously in 3D environments, mimicking the complex dynamics
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-the-art single-molecule microscopes in optical laboratories, as well as wet-chemical labs for sample preparation. The group is part of a bigger research cluster focusing on optical sensing. The surface
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lifetime is equally interdisciplinary, with a wide variety of activities ranging from art/science programmes, large scale science festivals, citizen science and educational initiatives at various levels
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is the covalent attachment of lipids to proteins, regulating their trafficking, protein–protein interactions, and stability. This post-translational modification is dynamically controlled by families