Sandoghdar max planck biography book

The research of our group aims to advance experimental and theoretical mastery of light-matter interaction at the nanometer scale and to achieve the same degree of control and finesse that is known from the gas-phase quantum optics in the condensed phase. To do this, we combine concepts from quantum optics, laser spectroscopy, cryogenics, optical imaging, scanning probe technology and nanofluidics.

In this endeavour, we have addressed a wide spectrum of scientific questions, ranging from quantum optics to biophysics. For more information, please consult our research website and our list of publications. Aggregation intermediates play a pivotal role in the assembly of amyloid fibrils, which are central to the pathogenesis of neurodegenerative diseases.

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The structures of filamentous intermediates and mature fibrils are now efficiently determined by single-particle cryo-electron microscopy. We report an atomic-resolution structural characterization of a toxic pre-fibrillar aggregation intermediate I1 on pathway to the formation of lipidic fibrils, which incorporate lipid molecules on protofilament surfaces during fibril growth on membranes.

Super-resolution microscopy reveals a tetrameric state, providing insights into the early oligomeric assembly. Time-resolved nuclear magnetic resonance NMR measurements uncover a structural reorganization essential for the transition of I1 to mature lipidic L2 fibrils. These structural insights have implications for the development of therapies and biomarkers.

Haselwandter, Roderick McKinnon. This study shows that five membrane proteins—three GPCRs, an ion channel, and an enzyme—form self-clusters under natural expression levels in a cardiac-derived cell line.

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The cluster size distributions imply that these proteins self-oligomerize reversibly through weak interactions. When the concentration of the proteins is increased through heterologous expression, the cluster size distributions approach a critical distribution at which point a phase transition occurs, yielding larger bulk phase clusters. A thermodynamic model like that explaining micellization of amphiphiles and lipid membrane formation accounts for this behavior.

We propose that many membrane proteins exist as oligomers that form through weak interactions, which we call higher-order transient structures HOTS.