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Description Thinking of doing your PhD in the Life Sciences? The International PhD Programme (IPP) Mainz is offering talented scientists the chance to work on cutting edge research projects within the open call on “Molecular Mechanisms in Genome Stability & Gene Regulation”. As an IPP PhD...
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an exciting interdisciplinary research environment at the interface of physics and biology. Our goal is to understand biological function and the role of condensates in disease by applying physical principles
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disrupt gene expression and stress responses. Using cutting-edge molecular and cellular biology approaches, in particular quantitative proteomics, we aim to uncover the mechanisms by which cells repair
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Description The Spemann Graduate School of Biology and Medicine (SGBM), University of Freiburg, is currently recruiting international PhD candidates for one doctoral position in the following
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a combination of biochemical reconstitution, biophysical characterization and structural biology (including AlphaFold predictions and cryo-Electron Microscopy), we will investigate the formation
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provides high‑level interdisciplinary training, international mobility, and excellent career development opportunities. It brings together leading groups at the interface of physics, chemistry, biology, and
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knowledge while at the same time promoting cultural and scientific understanding between the two regions. The research grants cover a wide range of topics - from molecular biology and garden architecture
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of biochemistry, structural biology, biophysics, cell biology, chemical biology and synthetic biology? The International Max Planck Research School for Living Matter: from molecules to dynamics (IMPRS-LM) is a
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. Research areas: Cell and Molecular Biology * Developmental Biology Vascular Biology * Immunology Biophysics * Neurobiology In vivo Imaging * High Resolution Optical Imaging and more. Applications for the PhD
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crystallography or Cryo-EM, quantitative/biophysical protein interaction studies, spectroscopy and molecular biology. We recently showed that WDR5, a component of the CLOCK/BMAL1 co-activating MLL1 histone