<p><strong>Heck is internationally recognized as one of the absolute pioneers in the use of mass spectrometry for large-scale protein research (proteomics). He has mentored many students and postdocs, several of them from the Czech Republic.</strong></p>
<h5><strong>You are a perfect example of a modern scientist, excelling in both research and science communication. How did you get started? What was your motivation to share your work with a broader audience?</strong></h5>
<p>My motivation for sharing science comes from being genuinely enthusiastic about my field of research, which can be quite specialised and complex. However, I believe it&#39;s crucial to share this enthusiasm not only with fellow scientists but also with the broader community, including neighbors, younger people and even children. As a scientist studying proteins, I find them fascinating, considering they are prevalent in our bodies and the entire world. My aim is to make more people appreciate the world of proteins by understanding them better.</p>
<p>Regarding my proficiency in science communication, I&#39;m not sure if I am really good. Initially, I found it challenging to effectively convey complex ideas to a broad audience. However, I&#39;ve learned that collaborating with individuals who are genuinely interested in science and experts in other fields like communication or art, can be incredibly helpful. They can play a crucial role in helping translate my scientific messages into presentations, videos, or social media posts. Working together, we bridge the gap between specialised knowledge and public understanding, making science more accessible and engaging for everyone. That&#39;s my motivation and approach to science communication.</p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Forum_Bas_van_Breukelen_Bridging_the_world_of_science_and_everyday_life_f241fc64fc/Forum-Bas-van-Breukelen-Bridging-the-world-of-science-and-everyday-life.jpg" alt="Forum/Bas van Breukelen: Bridging the world of science and everyday life"/></p>
<h5><strong>I really like the way you connect science and art. That you together with artists try to communicate your research in an innovative way, for example using dance. How did that start?</strong></h5>
<p>I generally think that science and art are not so different and both try to make or see something that&#39;s really beautiful. In our case, if you see how a living cell works, it&#39;s really beautiful. It is as beautiful as seeing a painting of Rembrandt. However, when you look at the painting of Rembrandt or when you look at the cell, it&#39;s not only about looking at it, it&#39;s also about interpreting. Both science and art tell stories behind what we see.</p>
<p>If you connect with artists who are on that same wavelength as you then it works. In making these dance movies, I was lucky to get connected with a team of young video artists who were really interested in science. And I just told them a story about what I study and what I really like, and then I gave them almost full freedom to make an interpretation. And they came up with ideas, we came up with ideas and then together we made something which is neither just art nor just a scientific publication, but it&#39;s something in between.</p>
<p>I quite like the fact that many more people saw that movie than have read my papers and I also feel that quite a few more people took something from that movie. Because I&#39;m not sure if the general public takes a lot from our papers. So I see it as a fun thing to do, which also provides added value making science more accessible.</p>
<h5><strong>Is it challenging to find the right balance between scientific accuracy and art?</strong></h5>
<p>It is and it isn&#39;t. The simple answer is yes, it&#39;s difficult. But if you start to think longer about it, you know, we scientists, when we have written a paper or report, we think this is the ground truth and that it will be valid for the next 50 years or so. And then next year, someone else makes a new measurement or a new discovery and comes up with a new interpretation. Even science itself is fact-based understanding. When you move into a more arty presentation of your science, you have to compromise because proteins are not visible by eye and so on. You need to make cartoons that show how they might look, which is close to reality, but not the real reality. So you have to make compromises. But if that means that more people get an idea and an understanding of what you want to say, then I think it&#39;s not so difficult to make these compromises.</p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Forum_Bas_van_Breukelen_Heck_s_lab_2ea8cc4c34/Forum-Bas-van-Breukelen-Heck's-lab.jpeg" alt="Forum/Bas van Breukelen: Heck&#39;s lab"/></p>
<h5><strong>Do you think that every scientist should communicate their research to the general public?</strong></h5>
<p>No, I think the science community should, but every person is different and you should not force every scientist to do science communication. But I think you should value when you have at your institute or in your group people who want to do it. And I think it&#39;s also extremely good to collaborate with people who are bridging the world of science and everyday life, who help scientists express their results to the general public in the most effective and engaging way. Some scientists are not good at science communication themselves but even their messages should be communicated. </p>
<h5><strong>You are also very active on <a href="https://twitter.com/hecklab">Twitter</a>. What&#39;s your motivation? Do you know how much time you spend on Twitter?</strong></h5>
<p>I think my motivation is not so different from many people that are on Twitter. Of course, it costs a bit of time. But I see many benefits. Sometimes I pick up things from Twitter that make me start to read the paper that I otherwise would not have read, or I hear about developments that I otherwise would not have heard about. And it&#39;s sort of broadening your network. However, you should also realise there is a bias. You don&#39;t reach everyone and not everyone reaches you, but it&#39;s just a fun way to keep connected with other scientists and maybe also with beyond science. </p>
<h5><strong>I know you really value diversity. Your team consists of many nationalities and types of expertise. Is this multidisciplinary approach the key to success?</strong></h5>
<p>The simple answer is yes. My group currently consists of 19 nationalities, several religions and gender classes. It is not the only or mandatory way, but I think for my group and for my science it really helps to have people from different backgrounds from different cultures, scientific expertise or social skills. They get along very well.</p>
<p>And I think when people leave the group, they have learned something in science, but they have also learned lessons in life. And maybe that&#39;s even better - a Chinese person learns from an American person and vice-versa or a chemist learns from a biologist and vice versa. This is very inspiring and enriching.</p>
<p>If you stay the whole life in the village where you were born and you only see that, you think that&#39;s normal. And I have learned that in the world, everyone thinks that their life is normal. But there are many different normals in the world and everything has its good and bad things. And I must say from my own experience that I have learned most about my own country while traveling abroad. Because you start to learn how your own country looks from the perspective of other countries and other cultures.</p>
<h5><strong>How important is networking for scientists and how do you build your own network? Do you have any tips or recommendations?</strong></h5>
<p>A good network is crucial. What I&#39;ve learned over the years is that the personal click is very important and you might have a scientist that may be the perfect fit in expertise, but if you don&#39;t like each other, then it&#39;s difficult. As a scientist, you may click with people all over the world. It doesn&#39;t need to be someone in your department. Science is a global thing, and that&#39;s the good thing about it.</p>
<p>What I really like about mass spectrometry is that we sometimes can help other scientists and of course, it makes you happy, but the real benefit for me is free education. Because if I talk to a neuroscientist, I will learn about neurology, if I talk to a physical chemist, I will hear about physical chemistry and so on. When you give something, you always get something back and I think this helps your own development and enriches your research. So I would recommend escaping our own ivory tower and start networking.</p>
<h5><strong>Many Czechs have worked in your group. Do you also collaborate with any Czech groups?</strong></h5>
<p>Yes, there were many Czech students or postdocs. And it is bad to generalize but I must say that all of them were smart and hardworking. In the last five years, I have been coordinating an European large-scale proteomic program. In this program we try to involve people from many countries, so there are also several Czech groups involved. The program is really nice because we get money to let people move from one lab to another and share information and knowledge. So it doesn&#39;t mean that we see each other every day, but we certainly have these connections.</p>
<blockquote>
<h5><strong>The trio of Czechs in Heck&#39;s lab</strong></h5>
</blockquote>
<blockquote>
<ul>
<li><strong>Jan Fiala</strong> (left) is a postdoc working on the development and application of mass spectrometry techniques for the study of archaeal organisms living in extreme environments such as hydrothermal vents or the Dead Sea. He received his PhD from the Faculty of Science of Charles University under the supervision of Petr Novák in 2021.</li>
</ul>
</blockquote>
<blockquote>
<ul>
<li><strong>Marta Siborová</strong> is a second-year postdoc in Heck&#39;s team. She uses cryo-electron microscopy to map interactions between human viruses and antibodies. She studied at Masaryk University in Brno. Her PhD thesis supervisor was structural virologist Pavel Plevka, who is currently also the director of CEITEC.</li>
</ul>
</blockquote>
<blockquote>
<ul>
<li><strong>Tereza Kadavá</strong> completed her Master&#39;s studies at the Faculty of Science of Charles University under a supervision of Petr Novák last year. As a PhD student in Heck&#39;s lab, she uses mass spectrometry-based techniques to study blood serum glycoproteins.</li>
</ul>
</blockquote>
<blockquote>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Forum_Bas_van_Breukelen_The_trio_of_Czechs_in_Heck_s_lab_bef263276d/Forum-Bas-van-Breukelen-The-trio-of-Czechs-in-Heck's-lab.jpeg" alt="Forum/Bas van Breukelen: The trio of Czechs in Heck&#39;s lab"/></p>
</blockquote>
<h5><strong>I read a few interviews with you and in one of them you mentioned that you are proud of watching young people come into your group, get trained, grow and mature. Do you know the statistics? How many scientists have you trained?</strong></h5>
<p>It depends. It always has to be nuanced, because who did I train? But just to give you a few numbers, in the 25 years that I&#39;ve been here, my lab has had over 100 PhD students graduating, about 75 postdocs and of course a lot of master students. We still have a network of alumni and about every five years we try to get everyone back. But they are all over the world now, some of them have remained in academia and are professors now, which I&#39;m proud of, but I&#39;m equally proud of alumni who work in industry or went into teaching.</p>
<p>When people ask me how I manage this group, I typically say I don&#39;t. And that it&#39;s the group that manages itself. Sometimes you can give a little shift here and a little direction there, but you have to get an atmosphere where people get trained by their buddy next to them and are in turn training other people. So the training is not something I can really put on my personal record, but I&#39;m proud of my group.</p>
<h5><strong>I also liked the fact that your next big question is what we can answer with mass spectrometry. Could you be more specific? What&#39;s your current next question?</strong></h5>
<p>My research has focused on mass spectrometry and you might say &#39;Hey, that&#39;s boring&#39; because that technology has already been around for more than 125 years. But I love it because every five years new things arise that maybe none of us who are the experts in the field had expected, which shows how dynamically and quickly this field is still moving. Things that we never thought that would happen are reality now. That we can study single cells with mass spectrometry, the proteome, the metabolome. For me, as a technology nerd, that&#39;s just amazing.</p>
<p>When I started my career, or even 10 years ago, I would have laughed if you had proposed that. I&#39;ve learned not to care about what is or isn&#39;t currently possible. And that&#39;s my message also to scientists: don&#39;t care. Just have visions of what you want to do and maybe one day it will be possible, and ideally you will have contributed to making this possible.</p>
<h5><strong>Do you have any other recommendations for young scientists?</strong></h5>
<p>If you&#39;re young, you should consider yourself &#39;a sponge&#39; and you should absorb, absorb, and absorb. Keep a broad perspective, learn about different disciplines. And maybe 20 years later you will really appreciate this knowledge. When you get older your sponge effect becomes weaker and you get stuck in what you were taught or what you believe. And I think staying young is maybe also about remaining such a sponge and being able to absorb things that are out of your comfort zone. So my recommendation is to remain a sponge.</p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Forum_Bas_van_Breukelen_Albert_Heck_from_Utrecht_University_fd0aed31dc/Forum-Bas-van-Breukelen-Albert-Heck-from-Utrecht-University.jpg" alt="Forum/Bas van Breukelen: Albert Heck from Utrecht University"/></p>
<h5><strong>What does your typical work day look like? Do you have any rituals, such as starting the day by reading the newspaper?</strong></h5>
<p>No, I think it&#39;s a bit boring to tell you the truth. My day starts by checking emails and that takes a lot of time. But I don&#39;t see it only as a burden, of course, since half of the emails are also your network and your information.</p>
<p>If I ask my children, they always say, oh, the only thing he does is drink coffee and talk to other people, which is sort of true. And there is never a typical day because every day is different. But what I find most fun is interacting with the students. But I also like to keep up my network with international scientists, and also with people in industry. So especially at this stage of my career my daily work really is keeping the network going, keeping the infrastructure going. From time to time, I have a sabbatical day where I think about where I want to go with the science of the group, and these are the most joyful moments. But as a leader of a group, there are many other duties to deal with, such as people in your lab having personal issues or problems finding housing or getting a visa, getting recommendations, nor should you underestimate teaching, that&#39;s also quite a bit of your time and it&#39;s important. As a scientist, I find it fun, but you have a lot of different tasks, so I think there&#39;s almost no typical day, and it&#39;s certainly not a routine.</p>
<h5><strong>You&#39;re a very passionate scientist, but if you were not a scientist, what would you be?</strong></h5>
<p>That&#39;s an interesting question. I like nature and I like to run and cycle and I especially like to travel, discovering new places and what people from other nations think but also to learn about myself and my own country. So if I had a free choice, I would be a traveler, I think.</p>
<blockquote>
<h4><strong>Professor Albert Heck</strong></h4>
</blockquote>
<blockquote>
<p>Albert Heck is a Distinguished Faculty Professor at the Science Faculty of Utrecht University, the Netherlands, and Scientific Director of the Netherlands Proteomics Centre. He studied chemistry at the Vrije Universiteit in Amsterdam and received his PhD in 1993 from the University of Amsterdam. After postdoc positions at Stanford University (US) and the University of Warwick (UK), he was appointed professor at Utrecht University at the age of 33. His group develops and implements innovative mass spectrometric methods for more efficient and detailed characterization of proteins in relation to their biological function, spanning the fields of proteomics, glycoproteomics and structural biology. He has received numerous awards, including the prestigious Spinoza Award of the Netherlands Organization for Scientific Research. He also received the Sir Hans Krebs Medal during the FEBS conference held in Prague in 2018.</p>
</blockquote>


Bridging the world of science and everyday life

<p><strong>Structural virologist Pavel Plevka, a two-time ERC grant holder and head of a research group at CEITEC Masaryk University, is looking for new colleagues to join his team. Even if you are not a structural virologist seeking an inspiring research environment, this interview is worth reading. Pavel Plevka explains his focus on studying human viruses and bacteriophages, his approach to team leadership, and the opportunities available for students and postdoctoral researchers who want to work in CEITEC's international and interdisciplinary research environment.</strong></p><h5><strong>Most people fear viruses and see them as something that causes problems. However, you look at viruses very closely in the lab, literally. What is so fascinating about structural virology that you have been awarded two ERC grants for research in this field?</strong></h5><p>Studying viruses through structural methods—nowadays primarily cryo-electron microscopy—fascinates me because it allows us to uncover previously unknown biological landscapes. Each virus is a precisely assembled nanoparticle, honed by millions of years of evolution to infect host cells with remarkable efficiency. By examining viral structures and their interactions with host cells, we can dissect the key steps of the infection cycle: how viruses enter cells, hijack their machinery, and ensure the production of progeny virions. Investigating these processes at molecular or even atomic resolution not only satisfies my scientific curiosity (laughs) but also holds promise for developing novel antiviral therapies.</p><p>I received ERC grants thanks to a combination of advanced structural biology methods and a strong focus on studying human pathogens. The scientific questions we address go to the heart of viral life: What does a viral particle look like, and how does it function? How does a virus penetrate a host cell and deliver its genetic material? How does it ensure the replication of its genome? How does it evade the host's defence mechanisms? How are new viral particles assembled from individual components? Structural biology enables me to answer these questions, and our findings may contribute to the fight against viral infections—an ongoing motivation for my work.</p><h5><strong>What was your path to structural virology?</strong></h5><p>I became interested in viruses in high school. When I found out that there was a virology group led by Associate Professor Jitka Forstová at the Faculty of Science at Charles University, it was an obvious choice for me. During my PhD studies in Sweden, I learned to use X-ray crystallography to determine viral structures, and as a post-doc in the U.S., I applied cryo-electron microscopy for the same purpose. Thanks to technological advances, cryo-electron microscopy and tomography are now the main techniques used by my research group.</p><h5><strong>CEITEC of Masaryk University is known for its state-of-the-art research equipment. What laboratory methods and technologies do you use to study virus structures?</strong></h5><p>As I mentioned earlier, we use primarily cryo-electron microscopy (cryo-EM), which allows us to examine the structure of viruses at atomic resolution. Additionally, tomography enables us to observe the infection process within cells. Since CEITEC is part of the Czech Infrastructure for Integrative Structural Biology (CIISB), we have access to cutting-edge equipment that facilitates our research and allows us to keep up with the world's leading laboratories.</p><p>Beyond cryo-EM, we also use molecular biology methods for recombinant protein production, CRISPR-Cas systems for modifying host cell and viral genomes, and biochemical techniques that help us understand the interactions between viral proteins and their receptors or antibodies.</p><h5><strong>What is the future direction of structural virology, and what innovations can we anticipate in the coming years?</strong></h5><p>Structural virology is shifting from simply characterizing viral particle structures to describing the molecular mechanisms of viral infection. From a technological standpoint, cryo-electron microscopy is indispensable, as its continuously improving resolution allows for increasingly detailed insights into virus interactions with cellular components. Cryo-electron tomography (cryo-ET) enables us to reconstruct three-dimensional structures of infected cells and observe the impact of viral infections in situ. For instance, observing how enteroviruses exploit membrane vesicle rupture during infection to enter the cytoplasm was fascinating.</p><p>I am also particularly interested in studying bacteriophages, which function as remarkable molecular machines. Our research explores bacteriophages as a potential therapeutic alternative to antibiotics, particularly for treating infections caused by antibiotic-resistant bacteria. Their ability to selectively target specific bacterial strains without affecting other cells makes them a promising tool for future personalized medicine, opening exciting opportunities for integrating virology with medical research.</p><h5><strong>What do you consider to be your team's most significant achievement so far? Is there a specific discovery that you are particularly proud of?</strong></h5><p>I am always delighted when someone in our group makes a discovery, regardless of its perceived significance, as the importance of a finding is often subjective. This makes it difficult to single out any one discovery. However, I am particularly proud of our research on enteroviruses, where we demonstrated how they enter host cells and release their genome from the viral particle into the cytoplasm. Our work on bacteriophage structures and their intricate mechanisms for hijacking bacterial cells to produce progeny is equally fascinating.</p><h5><strong>Your team gives the impression of being a well-tuned machine. How do you collaborate?</strong></h5><p>I place great importance on ensuring that my research group functions effectively. Selecting the right collaborators is crucial; I strive to bring in students and post-docs who are internally motivated and capable of working constructively with colleagues. Clear communication within the group is essential, so I try to be accessible and approachable. As a team, we meet twice a week. One meeting is dedicated to discussing articles relevant to our research, while the other features two group members presenting updates on their projects. After this meeting, I hold one-on-one discussions with each presenter to address challenges related to their work and set future directions.</p><p>Additionally, as part of CEITEC's annual staff evaluation process, I meet individually with each group member to discuss their working conditions and professional development. To foster a positive team environment, we organize a non-work-related, one-day teambuilding event twice a year and hold several group dinners throughout the year, often accompanied by board games, movie nights, or barbecues.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Pavel_Plevka_Zadavam_kolegum_z_tymu_jen_takove_projekty_na_kterych_bych_chtel_sam_pracovat_8fda0a1b81.jpg" alt="CEITEC: Pavel Plevka: I only give my team colleagues projects that I would be happy to work on myself" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Pavel_Plevka_Zadavam_kolegum_z_tymu_jen_takove_projekty_na_kterych_bych_chtel_sam_pracovat_8fda0a1b81.jpg 234w," sizes="100vw" width="1920" height="1280"></p><h5><strong>What qualities and skills do you look for in new team members? Who are you currently looking for?</strong></h5><p>My group's research focuses on the structural characterization of viruses and their replication cycle within infected cells. Ideally, I seek colleagues with experience in virology and cryo-electron microscopy; however, such specialists are rare worldwide. Therefore, I am interested in motivated and curious individuals eager to learn structural biology and unafraid of working with human pathogens. I value prior international research experience, as my time in Sweden and the U.S. has shown me how it broadens one's perspective, though it is not a requirement. We are looking for PhD students and post-docs to join our team.</p><h5><strong>What opportunities do you offer to candidates who want to join your team?</strong></h5><p>Our team offers the opportunity to participate in studies on viral structures and infection mechanisms. I believe it is essential to assign only those projects that I would personally find engaging. While projects are assigned individually, I encourage team members to collaborate and assist each other in solving specific methodological challenges. A major advantage of CEITEC is access to state-of-the-art technologies housed in shared laboratories. The experts in these facilities have extensive experience with instrumentation and data analysis, significantly accelerating our research. The most relevant facilities for our group include cryo-electron microscopy, light microscopy, macromolecular characterization, and mass spectrometry labs.</p><p>In addition to research work, I expect each group member to attend one or two conferences or training courses annually. My group is currently involved in ERC-Consolidator BioPhage, the National Institute of Virology and Bacteriology (NIVB), and NETPHARM projects.</p><h5><strong>The fundamental trait of a good scientist is natural curiosity, the drive to "go just a little further." What scientific challenges do you plan to tackle in the coming years?</strong></h5><p>I mentioned my group's current research topics earlier in this interview. Our new projects build upon them and include characterizing bacteriophage spread within biofilms using light-sheet fluorescence microscopy and genetically modified phages; describing bacteriophage replication directly in cells using a novel system that allows us to bypass the need for complex preparation of ultrathin samples for transmission electron microscopy; studying the mechanisms of tick-borne encephalitis virus neutralization and activation by antibodies; determining the mechanism of endosomal membrane rupture and its role in non-enveloped virus cell entry; and we also work to resolve the structures of viruses that infect less-studied organisms, such as ciliates.</p>

Pavel Plevka: I only give my team colleagues projects that I would be happy to work on myself

<p><a target="_blank" rel="noopener noreferrer" href="http://www.kva.se/en/"><strong>The Royal Swedish Academy of Sciences</strong></a> has decided to award the Nobel Prize in Chemistry 2025 to</p><p><strong>Susumu Kitagawa</strong>, born 1951 in Kyoto, Japan. PhD 1979 from Kyoto University, Japan. Professor at Kyoto University, Japan.</p><p><strong>Richard Robson</strong>, born 1937 in Glusburn, UK. PhD 1962 from University of Oxford, UK. Professor at University of Melbourne, Australia.</p><p><strong>Omar M. Yaghi</strong>, Born 1965 in Amman, Jordan. PhD 1990 from University of Illinois Urbana-Champaign, USA. Professor at University of California, Berkeley, USA.</p><p><i><strong>“for the development of metal-organic frameworks”</strong></i></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/The_Royal_Swedish_Academy_of_Sciences_Ill_Niklas_Elmehed_Nobel_Prize_Outreach_79e534fe53.jpg" alt="The Royal Swedish Academy of Sciences / Ill. Niklas Elmehed © Nobel Prize Outreach" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_The_Royal_Swedish_Academy_of_Sciences_Ill_Niklas_Elmehed_Nobel_Prize_Outreach_79e534fe53.jpg 234w," sizes="100vw" width="2560" height="1707"></p><h3><strong>Their molecular architecture contains rooms for chemistry</strong></h3><p><strong>The Nobel Prize laureates in chemistry 2025 </strong>have created molecular constructions with large spaces through which gases and other chemicals can flow. These constructions, <i>metal-organic frameworks</i>, can be used to harvest water from desert air, capture carbon dioxide, store toxic gases or catalyse chemical reactions.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_1_11e55a1d24.jpg" alt="©Johan Jarnestad / The Royal Swedish Academy of Sciences" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_1_11e55a1d24.jpg 229w," sizes="100vw" width="1529" height="1043"></p><p><strong>Susumu Kitagawa</strong>, <strong>Richard Robson</strong> and <strong>Omar Yaghi</strong> are awarded the Nobel Prize in Chemistry 2025. They have developed a new form of molecular architecture. In their constructions, metal ions function as cornerstones that are linked by long organic (carbon-based) molecules. Together, the metal ions and molecules are organised to form crystals that contain large cavities. These porous materials are called metal-organic frameworks (MOF). By varying the building blocks used in the MOFs, chemists can design them to capture and store specific substances. MOFs can also drive chemical reactions or conduct electricity.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_2_6eb99499cd.jpg" alt="©Johan Jarnestad / The Royal Swedish Academy of Sciences" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_2_6eb99499cd.jpg 235w," sizes="100vw" width="1479" height="983"></p><p><i>“Metal-organic frameworks have enormous potential, bringing previously unforeseen opportunities for custom-made materials with new functions,”</i> says <strong>Heiner Linke</strong>, Chair of the Nobel Committee for Chemistry.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_3_5f5c1f68b8.jpg" alt="©Johan Jarnestad / The Royal Swedish Academy of Sciences" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_3_5f5c1f68b8.jpg 245w," sizes="100vw" width="1529" height="768"></p><p>It all started in 1989, when <strong>Richard Robson</strong> tested utilising the inherent properties of atoms in a new way. He combined positively charged copper ions with a four-armed molecule; this had a chemical group that was attracted to copper ions at the end of each arm.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_4_961a149333.jpg" alt="©Johan Jarnestad / The Royal Swedish Academy of Sciences" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_4_961a149333.jpg 245w," sizes="100vw" width="1500" height="730"></p><p>When they were combined, they bonded to form a well-ordered, spacious crystal. It was like a diamond filled with innumerable cavities.</p><p>Robson immediately recognised the potential of his molecular construction, but it was unstable and collapsed easily. However, <strong>Susumu Kitagawa </strong>and <strong>Omar Yaghi</strong> provided this building method with a firm foundation; between 1992 and 2003 they made, separately, a series of revolutionary discoveries. Kitagawa showed that gases can flow in and out of the constructions and predicted that MOFs could be made flexible. Yaghi created a very stable MOF and showed that it can be modified using rational design, giving it new and desirable properties.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_5_bb8c4ba816.jpg" alt="©Johan Jarnestad / The Royal Swedish Academy of Sciences" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_5_bb8c4ba816.jpg 245w," sizes="100vw" width="1500" height="884"></p><p>Following the laureates’ groundbreaking discoveries, chemists have built tens of thousands of different MOFs. Some of these may contribute to solving some of humankind’s greatest challenges, with applications that include separating <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?search=PFAS"><strong>PFAS from water</strong></a>, breaking down traces of <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?categoryItems=1&amp;search=drugs"><strong>pharmaceuticals in the environment</strong></a>, capturing carbon dioxide or harvesting water from desert air.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_6_4cd7fb5f3b.jpg" alt="©Johan Jarnestad / The Royal Swedish Academy of Sciences" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Johan_Jarnestad_The_Royal_Swedish_Academy_of_Sciences_6_4cd7fb5f3b.jpg 167w," sizes="100vw" width="2480" height="2312"></p><h3><strong>Read more about this year’s prize</strong></h3><blockquote><ul><li><a target="_blank" rel="noopener noreferrer" href="https://www.nobelprize.org/uploads/2025/10/popular-chemistryprize2025-1.pdf">Popular science background: They have created new rooms for chemistry (pdf)</a>&nbsp;</li><li><a target="_blank" rel="noopener noreferrer" href="https://www.nobelprize.org/uploads/2025/10/advanced-chemistryprize2025.pdf">Scientific background to the Nobel Prize in Chemistry 2025&nbsp;(pdf)</a></li></ul><p><strong>Prize amount</strong>: 11 million Swedish kronor to be shared equally between the laureates<br><strong>Further information</strong>: www.kva.se and www.nobelprize.org<br><strong>Press contact</strong>: Eva Nevelius, Press Secretary, +46 70 878 67 63, eva.nevelius@kva.se<br><strong>Expert</strong>: Olof Ramström, +46 70 433 42 60, ramstrom@protonmail.com, member of the Nobel Committee for Chemistry</p></blockquote><p>The Royal Swedish Academy of Sciences, founded in 1739, is an independent organisation whose overall objective is to promote the sciences and strengthen their influence in society. The Academy takes special responsibility for the natural sciences and mathematics, but endeavours to promote the exchange of ideas between various disciplines.</p>

The Nobel Prize in Chemistry 2025 (live)

<p><strong>Thanks to her victory in the national round of the Falling Walls Lab science communication competition, the physical chemist Veronika Šedajová from CATRIN took part in the global finale in Berlin in early November. A total of one hundred finalists competed for the title Science Breakthrough of the Year in the Emerging Talents category. This global, interdisciplinary contest gives students and early-career researchers the opportunity to present their innovative ideas in just three minutes. Participants presented their research and proposed solutions to an expert jury made up of representatives from academia, industry and the public sector.</strong></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CATRIN_Falling_Walls_0416ccf355.jpg" alt="CATRIN: Falling Walls Lab" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CATRIN_Falling_Walls_0416ccf355.jpg 245w," sizes="100vw" width="2048" height="1094"></p><h4><strong>Veronika, what did you present in Berlin?</strong></h4><p>I presented our material—nitrogen-doped graphene for use in supercapacitors. I focused on the potential use of a supercapacitor containing our material in next-generation pacemakers and explained the benefits it could bring. I also mentioned that our research has already progressed from the lab towards practical application within the Trans2DChem project, and that we have founded the spin-out company Atomiver, where we are already able to produce the material in larger quantities.</p><h4><strong>As an experienced science communicator, what was different about this competition for you?</strong></h4><p>The format was very specific because of the extremely limited time. We were allowed only two slides and three minutes, which couldn’t be exceeded. So we were all under a lot of pressure to fit everything in. We presented before a jury made up of representatives of various scientific disciplines, so I had to make sure the information was understandable to everyone, not just colleagues from my field. It was important to show that the research is groundbreaking and to highlight its benefits for society.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CATRIN_Veronika_Sedajova_Finale_Falling_Walls_mi_rozsirilo_obzory_9789f8abb6.jpg" alt="CATRIN: Veronika Šedajová: The Falling Walls finale broadened my horizons" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CATRIN_Veronika_Sedajova_Finale_Falling_Walls_mi_rozsirilo_obzory_9789f8abb6.jpg 208w," sizes="100vw" width="1200" height="900"></p><h4><strong>Were you nervous? After all, it was the global finale with a hundred young scientists competing.</strong></h4><p>Given the significance and scale of the event, I was nervous—but I have to say I prepared for this competition more than for any other. I learned my script word for word to stay within the time limit. My colleague Martin Pykal helped me enormously by creating visualisations of what I wanted to present. I was also supported by the science communicator Vendula Lužná from Palacký University, as well as the community around the Žárovky endowment fund. It was extremely helpful to talk to Czech finalists from previous years, who gave me many useful recommendations. And I am very grateful to Barbora Boušová from the Czech office of DAAD: German Academic Exchange Service, who travelled with me to Berlin, for her support and encouragement.</p><h4><strong>How did you enjoy the presentations given by the other finalists?</strong></h4><p>It was very enriching to see what problems researchers from different countries around the world are tackling. From the follow-up discussions I also learned what kind of resources colleagues—for example in Africa or South America—do or do not have, and how they collaborate internationally. It really opens your eyes and gives you a new perspective. The event definitely broadened my horizons, and I plan to listen to the presentations again because I wasn’t able to fully concentrate on all of them. As I learnt later from conversations with the other finalists, I was actually quite easy to recognise thanks to my props—I had the supercapacitor that I carry with me everywhere and a large bottle of graphene.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CATRIN_Veronika_Sedajova_Finale_Falling_Walls_mi_rozsirilo_obzory_2_84f27d367b.jpg" alt="CATRIN: Veronika Šedajová: The Falling Walls finale broadened my horizons" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CATRIN_Veronika_Sedajova_Finale_Falling_Walls_mi_rozsirilo_obzory_2_84f27d367b.jpg 208w," sizes="100vw" width="1200" height="900"></p><h4><strong>The presentations took place over a single day, but together with the other finalists you could attend the whole Science Summit. What did that bring you?</strong></h4><p>We had a very demanding programme, during which we visited university departments and the laboratories of the Max Planck Institute. The weekend was dedicated to networking. We could attend any lectures we wanted, and there were dedicated networking sessions with representatives of major industrial players. You could talk to people from different sectors and possibly even find someone to collaborate with in the future. Many people were approaching us, so it was certainly very useful. I also met representatives of the Czech Embassy in Berlin and described our research to the ambassador.</p><h4><strong>Will science communication remain something you want to pursue alongside your research and company work? Was the competition a new impulse?</strong></h4><p>I’ve always enjoyed science communication, and to some extent it helps me push my own boundaries. I’m rather prone to stress, and events like this teach me to calm down and present science to people who are not experts. The advice we received in Berlin will definitely be useful in the future—whether when presenting scientific results or within a company. I still consider science popularization important, but I don’t have any special plans. I’m letting things flow—we’ll see.</p>

Veronika Šedajová: The Falling Walls finale broadened my horizons

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