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Hari Prakash Thanabalan will defend his PhD thesis on March 23rd, 2026.

Photograph of the soft robot, consisting of a multilayer rolled dielectric elastomer actuator integrated with a
flexible PET sheet. (Image by H. P. Thanabalan.)
Hari Prakash Thanabalan will defend his PhD thesis on March 23rd, 2026.
The defense will take place in PJ Salen lecture hall, Institutionen för fysik, Johanneberg Campus, Göteborg, at 13:00.

Title: Soft Robotic Platforms for Dynamic Conditions: From Adaptive Locomotion to Space Exploration

Abstract:
Inspired by living organisms, soft robots represent a significant advancement in robotics, offering exceptional flexibility and nearly infinite degrees of freedom. These properties make them ideal for unstructured and remote environments such as planetary surfaces. However, challenges remain in developing efficient and durable soft actuators capable of withstanding complex operational conditions. This work presents two interconnected parts.

In the first part, an inchworm-inspired soft robot was developed that is capable of controlled directionality through a passive alignment mechanism integrated with a 3D-printed grooved substrate. This design enables precise locomotion control using only a single rolled dielectric elastomer actuator (RDEA), eliminating the need for multiple actuators or complex control systems. Experimental validation confirms that manipulating groove angles on the substrate reliably guides locomotion, improving energy efficiency and mechanical simplicity.

In the second part, the fabrication and resilience of fault-tolerant RDEAs were tested. RDEAs utilising Single-Walled Carbon Nanotubes (SWCNTs) as compliant electrodes were developed to withstand multiple damages where they were tested for punctures and cuts. Additionally, the radiation tolerance of these actuators was evaluated under space-like conditions, including Galactic Cosmic Rays and Solar Particle Events, which expose materials to high-energy protons and alpha particles. A computational dual-simulation framework was applied, combining the Stopping and Range of Ions in Matter (SRIM) software for alpha particle interactions and ESA’s SPENVIS Multi-Layered Shielding Simulation Software (MULASSIS) for proton radiation effects.

This framework concerns material selection for robust RDEA fabrication aimed at extraterrestrial applications. Together, these projects advance the development of bioinspired soft robots with improved directional control and environmental resilience, supporting future applications in search and rescue, pipe inspection, and planetary exploration.

Thesis: https://hdl.handle.net/2077/90552

Supervisor: Giovanni Volpe
Examiner: Bernhard Mehlig
Opponent: Maria Guix Noguera
Committee: Juliane Simmchen, Hamid Kellay, Paolo Vinai
Alternate board member: Måns Henningson

 

Poster by P. Dutta at the Protein Folding in Real Time Conference, Stockholm, 11th March 2026

A coarse-grained molecular dynamics framework used to simulate plasmid DNA analyzed via atomic force microscopy (AFM). The resulting images are used to train a U-Net for DNA chain and crossing segmentation and classification. (Image by P. Dutta.)
ASAP (AFM Simulation and Analysis Pipeline)
Prakhar Dutta, Jiacheng Huang, Nazli Demirpehlivan, Thomas Catley, Sylvia Whittle, Carlo Manzo, Rahul Nagshi, Rachel Owen, Giovanni Volpe
Date: 11th March 2026
Time: 18:00 – 20:00
Place: Aula Medica, Karolinska Institute, Solna
Conference Protein Folding in Real Time, 11-13 March 2026, Stockholm, Sweden

Abstract: Atomic force microscopy (AFM) resolves biological structure and mechanics at high resolution, but produces vast, heterogeneous datasets that are often noisy and very time-consuming to analyse. Although deep learning could automate quality control, segmentation and feature extraction, adoption is limited by scarce ground-truth training data and high technical barriers for experimentalists. Here we present ASAP, an open-source tutorial and pipeline implemented in DeepTrack to provide a reproducible foundation for AI-enabled AFM. At the protein folding conference, a dual-pathway simulation for DNA, offering both molecular dynamics and rapid, non-MD geometries to generate perfect ground truth for segmentation training was presented. By consolidating simulation and learning into a single modular ecosystem, this work enables users to build upon our pipeline to optimize AFM workflows for more efficient data acquisition and robust processing.

Poster by X. Zhang at at the Protein Folding in Real Time conference, Stockholm, 11 March 2026

Reconstructed field of LCD2–CTPR4-Func1 condensates with LC3 at the sample plane (shown here as the imaginary component of the complex field). The condensates increase in size through Ostwald ripening and recruitment of LC3. (Image by X. Zhang.)
Quantitative Characterization of Biomolecular Condensates Using Off-Axis Holographic Microscopy
Xinwen Zhang, Nora Haanaes, Berenice García Rodríguez, Giovanni Volpe,  Janet Kumita and Daniel Midtvedt
Date: 11 March 2026
Time: 18:00-20:00
Place: Aula Medica, Karolinska Institute, Solna
Conference Protein Folding in Real Time, 11-13 March 2026, Stockholm, Sweden

Biomolecular condensates formed through liquid–liquid phase separation (LLPS) play important roles in cellular organization, yet quantitative and label-free characterization of their physical properties remains challenging. In this work, we apply off-axis holographic microscopy to study a synthetic biomolecular condensate platform based on the LCD2-CTPR protein system. These proteins, composed of modular consensus-designed tetratricopeptide repeat (CTPR) domains fused to intrinsically disordered regions, undergo phase separation under varying salt concentrations. By incorporating short binding motifs such as ATG13 or Func1, the condensates can specifically recruit the autophagy-related protein LC3. Using label-free quantitative phase measurements, we analyze changes in condensate optical radius and refractive index during LC3 recruitment and over time. Our results show measurable variations in condensate size and optical properties, highlighting the sensitivity of these systems to compositional changes. This work demonstrates the applicability of holographic microscopy for quantitative characterization of synthetic biomolecular condensates and provides a framework for studying protein phase separation in a non-invasive manner.

Poster by E. A. Duta Costache at the Protein Folding in Real Time conference, Stockholm, 11 March 2026

Pointwise absolute error plots for the heat equation tested across five architectures. The plots show the mean absolute error achieved by each architecture on a periodic-mode initial condition. Errors are shown on a logarithmic scale. Blue colors indicate smaller errors. (Image by E. A. Duta Costache.)
The optimization autopsy of PINNs
Eduard Duta Costache, Benjamin Girault
Date: 11 March 2026
Time: 18:00-20:00
Place: Aula Medica, Karolinska Institute, Solna
Conference Protein Folding in Real Time, 11-13 March 2026, Stockholm, Sweden

Physics-Informed Neural Networks (PINNs) have emerged as a promising method for solving Partial Differential Equations (PDEs) by combining data-driven learning with physical laws. However, the spectral bias and optimization challenges limit their efficacy. This work investigates these issues and whether the advantages of classical spectral methods translate to the non-convex neural network optimization landscape. We show that gradient imbalance greatly affect learning and we study the Hessian conditioning under different settings. Our results indicate that spectral priors stabilize training, reduce error, and improve parameter efficiency. We also identify that learnable-basis models act as implicit regularizers under sparse sampling.

Poster by Sreekanth K Manikandan at the Protein Folding in Real Time conference, Stockholm, 11 March 2026

Recent advances in nonequilibrium physics allow extracting thermodynamic quantities, such as entropy production, directly from dynamical information in microscopic movies. (Figure by S. Manikandan, adapted from Manikandan et al., Phys. Rev. Research 6, 023310 (2024).)
Probing the Non-equilibrium Dynamics of Living Matter
Sreekanth K Manikandan
Date: 11 March 2026
Time: 18.00-20.00
Place: Aula Medica, Stockholm Sweden
Conference Protein Folding in Real Time, 11-13 March 2026, Stockholm, Sweden

Identifying whether a process is in equilibrium, quantifying its distance from equilibrium, and constructing optimal reduced descriptions of non-equilibrium dynamics remain central challenges in the study of living matter. Here, we discuss how data-driven approaches grounded in stochastic thermodynamics enable these features to be inferred directly from experimental data. In particular, we show how entropy production can be localized in space and time, and how maximally dissipative coordinates emerge as effective low-dimensional descriptions of non-equilibrium processes. We highlight applications to experimental biophysical systems and discuss key challenges and limitations.

Poster by A. Schiano di Colella at the Protein Folding in Real Time conference, Stockholm, 11 March 2026

Schematic representation of the architecture of a quantum circuit for application in variational problems. (Image by A. Schiano di Colella.)
Quantum computing for variational problems
Andrea Schiano di Colella, Antonio Ciarlo, Mats Granath, Giovanni Volpe
Date: 11 March 2026
Time: 18:00 – 20:00
Place: Aula Medica, Karolinska Institutet, Stockholm, Sweden
Conference: Protein Folding in Real Time

Quantum computing is a field of study that aims to exploit quantum mechanical effects for the purposes of computation. Due to the intrinsic capacity of qubits of efficiently represent an exponentially large configuration space, quantum computation has been identified as a promising candidate for complex physical chemistry simulations, including investigating the dynamics of protein folding. This work illustrates the use of quantum computing for variational problems, and the use of alternative training methods such as genetic algorithms to avoid the “barren plateau” phenomenon, which prevents the training of general quantum circuits by means of the usual gradient descent.

Poster by N. C. Palmero Cruz at the Protein Folding in Real Time conference, Stockholm, 11 March 2026

3D model of the integrated setup combining optical tweezers, light-sheet microscopy, and microfluidics to manipulate the gut microbiome in vivo in zebrafish. (Image by N. C. Palmero Cruz.)
Optical Manipulation of Gut Microbiome and Neural Responses in Zebrafish
Norma Caridad Palmero Cruz
Date: 11 March 2026
Time: 18.00-20.00
Place: Aula Medica, Stockholm Sweden
Conference Protein Folding in Real Time, 11-13 March 2026, Stockholm, Sweden

The gut-brain axis is a complex, bidirectional network linking the microbiome to the central nervous system, significantly affecting physiological processes and neurological health, including conditions like autism and depression. Due to the genetic similarities between zebrafish and humans, the zebrafish serves as a valuable model for investigating the bidirectional relationship between the gut and brain, offering insights into how it compares with human behaviors. Research on the connection between gut and brain development typically involves using germ-free lab animals, where the microbiome is eliminated, and comparing them to those with restored microbiomes. However, this method does not capture the complexity of microbiome-nervous system communication due to its all-or-nothing approach. This work presents a setup that combines microfluidic techniques, optical tweezers, and light sheet microscopy to precisely manipulate the microbiome in larval zebrafish in situ and in vivo. This approach offers deeper insights into gut-brain connectivity and its impact on neurological health.

Poster by L. Viaene at the Protein Folding in Real Time conference, Stockholm, 11 March 2026

Heat-induced aggregates in Saccharomyces cerevisiae on Slimfield SMLM. Hsp104-mGFP binds to misfolded regions enabling aggregate visualisation for tracking. (Image by L. Viaene.)
A single-molecule approach to study the spatial protein quality control system
Linde Viaene
Date: 11 March 2026
Time: 18.00-20.00
Place: Aula Medica, Stockholm Sweden
Conference Protein Folding in Real Time, 11-13 March 2026, Stockholm, Sweden

Cell populations are inherently diverse, and averaging measurements across them can mask subtle or rare cellular behaviours. In this work, we use live Slimfield single-molecule microscopy to study the role of Hsp104 in clearing misfolded and aggregated proteins after stress. By analysing endogenously tagged Hsp104, we quantify molecular diffusion and stoichiometry before and after heat stress. Our results show a transition from faster, more mobile molecules to larger, more static assemblies following stress, consistent with Hsp104 functionally engaging with protein aggregates. These measurements provide molecular-level insight into how cells respond to proteotoxic stress.

International conference “Protein Folding in Real Time: From Molecules to Disease”, Aula Medica, KI, Stockholm, 11-13 March 2026

Giovanni Volpe opens the Protein Folding in Real Time conference. (Photo by A. Ciarlo)
The international conference Protein Folding in Real Time: From Molecules to Disease opened today, 11 March 2026, at Aula Medica, KI, Stockholm.

The conference brings together researchers from multiple disciplines, including biophysics, molecular biology, computational science, and medicine, to discuss recent advances in the study of protein folding. Proteins must fold into precise three-dimensional structures to perform their biological functions, and failures in this process are associated with several diseases, including neurodegenerative disorders and cancer.

During the three-day meeting, participants attend a series of lectures and discussions covering topics such as single-molecule biophysics, high-resolution experimental techniques for observing folding dynamics, advanced molecular simulations, and artificial intelligence approaches for predicting folding pathways. Particular attention is given to the challenge of observing protein folding in real time, capturing transient intermediate states that determine whether proteins reach their functional structure or misfold.

The event also highlights the interdisciplinary and international nature of the initiative. Representatives from the Embassies of Italy, Japan, and Spain, together with UNESCO, take part in the meeting, emphasizing the global interest in advancing research on protein folding and its biomedical implications. The initiative aims to integrate experimental measurements, computational modeling, and data-driven approaches to build a predictive framework for protein folding dynamics. By combining advanced imaging, force spectroscopy, and machine learning methods, the initiative seeks to better understand how folding processes occur inside living systems and how their disruption can lead to disease.

Overall, the conference provides an opportunity for scientists from different institutions to exchange ideas, establish collaborations, and shape future research directions in the field of protein folding and misfolding. The launch of this initiative represents an important step toward bridging molecular-level observations with biomedical applications, ultimately contributing to improved strategies for diagnosing and treating diseases related to protein misfolding.

Technological Excellence Requires Human and Social Context on ArXiv

Why breakthrough research needs humanities and social sciences. (From an artwork by Jacopo Sacquegno.)
Technological Excellence Requires Human and Social Context
Karl Palmås, Mats Benner, Monica Billger, Ben Clarke, Raimund Feifel, Julia Fernandez-Rodriguez, Anna Foka, Juliette Griffié, Claes Gustafsson, Kerstin Hamilton, Johan Holmén, Kristina Lindström, Tobias Olofsson, Joana B. Pereira, Marisa Ponti, Julia Ravanis, Sviatlana Shashkova, Emma Sparr, Pontus Strimling, Fredrik Höök, Giovanni Volpe
arXiv: 2603.10653

Breakthrough technologies increasingly shape social institutions, economic systems, and political futures. Yet models of research excellence associated with such technologies often prioritize technical performance, scalability, and short-term innovation metrics while treating ethical, social, and cultural dimensions as secondary considerations. This perspective article argues that such separation is no longer tenable. We propose a broader understanding of excellence that combines technical rigor with ethical robustness, social intelligibility, and long-term relevance. The rapid emergence of generative and agentic artificial intelligence further underscores this argument. As technological systems increasingly operate through language, interpretation, and normative alignment, expertise traditionally cultivated in the humanities and social sciences becomes integral to the design, governance, and responsible deployment of such systems. Drawing on historical examples and contemporary research practices, this article examines five interconnected domains where the humanities and social sciences, treated as integrated dimensions of research practice, can strengthen technological development: (1) ethical, legal, and social integration in agenda-setting and research design; (2) plural and reflexive foresight practices that shape technological futures; (3) graduate education as a leverage point for cross-disciplinary literacy; (4) visualization and communication as epistemic and civic practices; and (5) institutional frameworks that move beyond rigid distinctions between basic and applied research. Across these dimensions, we propose practical strategies for embedding interdisciplinary collaboration structurally rather than symbolically.