September 16th, 2025 at 12:15, room U1.191

SBBS introductory meeting for students 

If you missed the introduction meeting, feel free to contact one of the organisers by email or at the first seminar.

October 14th, 2025 at 12:15, room U1.197

Molecular Mechanisms Underlying the Energy Currents of Life

Biological energy conversion is catalyzed by gigantic membrane-bound protein complexes that transduce redox energy into a trans-membrane proton gradient, powering the synthesis of ATP. Yet, despite significant advances, the molecular principles of these long-range proton transfer reactions remain poorly understood, and a major scientific challenge. In this talk, I describe our integrative mechanistic exploration of biological energy transduction, where we combine biophysical, computational, and structural approaches to derive a molecular understanding of these intricate processes. I describe our recent work on the highly intricate Complex I machinery, catalyzing a >200 Å redox-driven proton transfer reaction. Our findings reveal that Complex I controls long-range proton transfer reactions by intrinsic electric field effects that result in conformational and hydration changes, mediated by allosteric effects. We find that mutations of key residues mediating this process results in a perturbed coupling effect that result in development of severe mitochondrial diseases. I will also discuss our recent work on addressing the function of respiratory supercomplexes, and how the formation of such molecular assemblies affects key protein-lipid interactions. On a general level, our findings reveal novel energy transduction mechanism, with striking similarities amongst different biological systems.

Prof. Dr. Ville Kaila

Department of Biochemistry and Biophysics (DBB), Stockholm University 

Stockholm, Sweden

November 11th, 2025 at 12:15, room U1.197

Mechanisms of nutrient sensing by the mTOR pathway

In this talk, I will discuss my lab’s recent discovery of two molecular mechanisms by which cells sense dietary nutrients—specifically, the amino acids leucine and arginine. I will guide you through the mTOR pathway, a central system that orchestrates this process. You will learn about the intricate cascade of signaling events, beginning with the detection of amino acids by specialized protein sensors, the relay of this information through the GATOR2 protein complex, and culminating in the activation of the large protein kinase mTOR. mTOR ultimately determines whether a cell builds biomass and grows or recycles existing resources and enters a standby mode until fresh nutrients are available. This talk will expose you to the remarkable role of proteins as signaling molecules, guiding cells in making critical growth decisions in response to environmental conditions.

Prof. Dr. Kacper Rogala

Departments of Structural Biology and Chemical & Systems Biology, Stanford University 

Palo Alto, CA, USA

November 18th, 2025 at 12:15, room U1.197

NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins involved in Viral Replication

Proteins are inherently dynamic, exhibiting conformational freedom on many timescales, implicating structural rearrangements that play a major role in molecular interaction, thermodynamic stability and biological function. Intrinsically disordered proteins (IDPs) represent extreme examples where flexibility defines molecular function. In spite of the ubiquitous presence of IDPs throughout biology, the molecular mechanisms regulating their interactions remain poorly understood. We use NMR spectroscopy to develop a unified description of the dynamics of IDPs as a function of environmental conditions, from membraneless organelles to in-cell, and to map these complex molecular recognition trajectories at atomic resolution, from the highly dynamic free-state equilibrium to the bound state ensemble. Examples include the nuclear pore, where weak interactions between the nuclear transporter and highly flexible chains containing multiple ultra-short recognition motifs, facilitate fast passage into the nucleus, the replication machinery of Measles virus, where we use NMR to characterize the 92 kDa complex formed between the highly disordered phosphoprotein and the nucleoprotein prior to nucleocapsid assembly – a process that we can also follow in real-time. These proteins undergo liquid-liquid phase separation upon mixing and we can combine NMR and fluorescence to describe the molecular basis and functional advantages of this phenomenon. NMR also sheds new light on the molecular basis of host adaptation of influenza polymerase, via a highly dynamic interaction, and reveals the dynamic assembly of SARS-CoV-2 nucleoprotein with its viral partner nsp3, and the role of hyperphosphorylation in the viral cycle.

Dr. Martin Blackledge

Institut de Biologie Structurale

Grenoble, France

December 2nd, 2025 at 12:15, room U1.197

TBA

Prof. Dr. Flemming Hansen

Institute of Structural and Molecular Biology, University College London

London, UK

December 9th, 2025 at 12:15, room U1.197

TBA
 

Prof. Dr. Kelly Nguyen

MRC Laboratory of Molecular Biology, UKRI

Cambridge, UK

December 16th, 2025 at 12:15, room U1.197

TBA
 

Prof. Dr. Bonnie Murphy

Department of Biophysics, MPI Frankfurt

Frankfurt, Germany