Dan Shechtman inspires young scientists in Nepal

I, on the behalf of the Asian Science Camp Alumni Association, have hosted an event “Interactive Session with Nobel Laureate Prof.Dr. Dan Schechtman” in a collaboration with the International Quasi Crystal Conference and Embassy of Israel In Nepal on 19th September 2016, at the Hotel Soltee Crown Plaza, in Kathmandu, Nepal.

 

Kathmandu's Durbar Square with the magnificent Bodnath Stupa in its center (picture was taken before the horrible earthquake in 215 struck the city). Photo: iStock.com/fotoVoyager

Kathmandu’s Durbar Square with the magnificent Bodnath Stupa in its center (picture was taken before the horrible earthquake in April 2015 struck the city). Photo: iStock.com/fotoVoyager

The hall of Hotel Soltee Crowne Plaza was jammed on 19th September with researchers, young scientists, students of various fields, political leaders from leading parties, government representatives and policy makers to attend the talk of Prof. Dan Shechtman. He stood among a huge crowd of unknown faces, yet expressed himself with such an amiable manner. Only few people possess such a down to earth and charismatic personality like Prof. Dan Shechtman. No doubt, the Nobel Laureates’ story is a fascinating one: from his achievements and the hard work he has done to the roller coaster ride of his eventual success.  In addition, Shechtman also shared many of his ideas, gave us insights on how he thinks and much more. Only few people get the chance to meet such a great personality and the young researchers, I must say, are very lucky to get this once in a life time opportunity to meet Prof. Dan Shechtman.

Since Dan Shechtman is a professor of material sciences and a Nobel Laureate in Chemistry, everyone expected him to talk about his scientific achievements and experiences. But out of the blue, he talked about another topic dear to his heart: the role of technological entrepreneurship for the development of a nation. The title of his speech was “Technological Entrepreneurship – A Key to World Peace and Prosperity”. He advocated the important role of techno-entrepreneurship in transforming developing countries like Nepal into efficient economies. He emphasized that developing entrepreneurial spirit and a well educated youth is paramount for the development of a country.

 

Nobel Laureate Dan Shechtman with attendees of his lecture. Photo: Asian Science Camp Alumni Association

Nobel Laureate Dan Shechtman with attendees of his lecture. Photo: Asian Science Camp Alumni Association

Professor Shechtman especially stressed the significance of good basic education for everyone. He listed good engineers, science education, proper government policy and anti-corruption measures as basic components that help empowering a country’s entrepreneurship. He also shared ideas and suggested some do’s and don’ts, e.g. regarding potential sources of investments and strategies for the startups. Shechtman then explained the situation in his home country Israel: “Israel is a small country with a small population and small markets. So the majority of our products are exports. If you produce products more efficiently, you can compete easily in foreign markets. When you come up with a new thing, it is innovation. When you turn your innovation into something marketable, that’s entrepreneurship.”

With his experiences at the Technion, Professor Shechtman showed the importance of science education for a nation. He further added: “Entrepreneurship does not come naturally to anyone. You have to teach it like you teach mathematics.” Shechtman illustrated his thoughts by bringing up relevant examples of the development of Israel, Taiwan and other comparable countries. Finally, the participants got a chance to ask their own question which was a dream coming true for everyone in attendance. Professor Shechtman’s speech was a real treat to all of us and many young Nepalese will take lots of inspiration from his speech.

The Story behind the Hype: Cockroach Milk

 The phone in S Ramaswamy’s office at the Institute for Stem Cell Biology and Regenerative Medicine (inStem) has been ringing off the hook. “Normally no-one calls my office,” says the Bangalore-based researcher. Ramaswamy had just talked to a TV channel about his recent research breakthrough. As we settle down for the interview, another reporter from a global news service calls to make an appointment for an interview. The story they were interested in has been 10 years in the making—a story that began when a young undergraduate student, Nathan Coussens, observed some crystals in the gut of an unborn Pacific beetle cockroach.

Commonly found in the landscapes of Hawaii, the Pacific beetle cockroach (Diploptera punctata) is the only known species of viviparous cockroach. This means that it gives birth to living young, not eggs, and the offspring are nourished by the mother in her brood sac. Studied in laboratories for many years now, these roaches have suddenly shot to stardom as the world’s next superfood source, mere weeks after a study published by Ramaswamy and his colleagues in IUCrJ, an open-access journal published by the International Union of Crystallography.

 

Nymph of the Pacific Beetle Cockroach. Photo: iStock.com/keeperofthezoo

Nymph of the Pacific Beetle Cockroach. Photo: iStock.com/keeperofthezoo

In the spring of 2006, Nathan Coussens, now a Senior Research Scientist at the National Institutes of Health (NIH), found a specimen of the Pacific beetle cockroach in the laboratory of Barbara Stay, at the University of Iowa. Stay, dubbed by colleagues as ‘Cockroach Lady’, had the largest collection of the world’s cockroaches during her time in Iowa. Coussens’ interest was piqued by the shiny crystals he saw in the gut of the cockroach. Stay had seen these crystals before. Crystals in the gut, when observed, are assumed to be crystals of urea or waste products that crystallise very readily. Coussens, however, had a hunch that these might be different. He took them to Ramaswamy, then a professor in the Department of Biochemistry at the University of Iowa, who studied crystal structures. Coussens put them in the x-ray beam and found, to everyone’s surprise, that these were proteins, not waste.

“Once we realised these were proteins, we were hooked,” said Ramaswamy, “we wanted to find out what these crystals are, understand the protein. It is actually nontrivial to get crystals grown in vivo (inside a living organism).” Naturally occurring protein crystals are rare—making proteins crystallise is usually a challenge for crystallographers—the researchers wanted to know what about the structure makes these different and understand their function at a molecular level. At 10-20 microns, the crystals were larger than the few known naturally-occurring protein crystals, but small enough to make structure determination using x-rays difficult.

When nothing is known about the structure of a protein, researchers resort to a nifty trick, one of the oldest in the book, which makes it possible to effectively use x-ray crystallography and solve the structure. One or more heavy atoms are introduced into specific sites in the crystal without disturbing its perfect repeating pattern. But the researchers were unable to incorporate heavy atoms in these crystals. Efforts at preparing the protein crystals for Nuclear Magnetic Resonance (NMR), a different technique for structure determination, also failed. They even wrote a proposal to NASA, who were conducting experiments to see if protein crystals could be grown better in space, to send the cockroaches to space. “We tried a number of interesting things and did it as a fun, really curious project,” said Ramaswamy.

With Ramaswamy’s move to inStem, Bangalore, the project took a backseat. However, in early 2013, Leonard Chavas, a scientist who had learnt about the project from Ramaswamy, was eager to initiate it again. With his easy access to SOLEIL, a synchrotron facility near Paris, France, where he manages a beam line named PROXIMA1 and heads the HelioBio section, Chavas was uniquely positioned to help solve the technical challenge of determining the structure of proteins contained in the micro crystals. “I work with new x-ray sources called x-ray free electron lasers. Using these x-ray sources, it is possible to work with very difficult samples,” said Chavas.

 

The technique that solved the structure is called Sulphur Single-wavelength Anomalous Diffraction (S-SAD). Chavas explains, “When you have difficulties solving a structure, it is good to work with atoms that are easier to see, that are bigger. For that, you need to introduce heavy atoms into the system, but that didn’t work here. However, sulphur is already present in most, if not all, proteins known so far. So if you are able to find a way to get a good signal from the sulphur, then you can use it as a pseudo heavy atom that helps you to solve the structure.” His team built a beam line at the Photon Factory, a synchrotron in Japan, which worked at an energy that could “see” the sulphur atoms. However, that was not the only challenge.

The packing or arrangement of the molecules in the crystal was, in crystallographer speak, space group P1. This, in Chavas’ words, “is the most difficult space group for structure studies because there is no symmetry between molecules.” Before this, no structure in P1 had been solved using S-SAD. “It helped that the crystals were so good. The data was actually very nice,” said Chavas.

Sanchari Banerjee, a postdoc in Ramaswamy’s lab worked with the team to analyse the data and solve the structure. They learnt that the crystals were unusual in many ways. These crystals were not made up of one protein, but three—they are heterogeneous, not homogeneous. This was so surprising that the researchers had to double-check their results using a second technique called mass spectrometry. “We crystallographers struggle hard in the lab making homogeneous protein samples to get crystals that will diffract well, and here nature has provided us heterogeneous crystals that diffract so well that we can see the atoms they’re made of. This is extremely fascinating,” said Banerjee. 

Bound to these proteins are sugars called glycans and molecules of fat, a combination of molecules akin to milk. The protein-rich liquid food provided by the mother cockroach, the researchers realised, had crystallised in the embryos’ guts, to be always readily available to the quickly growing offspring. The researchers are now busy expressing the protein in the bacteria, E. coli, and in yeast. The scientists, curious as ever, are keener to use the versatility of yeast as a molecular toolbox to learn more about the remarkable crystals, in particular to test whether their theories about what makes them crystallise so readily are accurate.

During their investigations, the researchers estimated, among other properties of the crystal, the calorific value. They found that “a single crystal is estimated to contain more than three times the energy of an equivalent mass of dairy milk.” The potential of harvesting the crystals as a source of nutrition has triggered tremendous interest in the popular press, many of them tapping into the “ick factor” that food made from cockroaches would provoke. In the last few weeks, the number of articles, TV stories and even Youtube videos “have multiplied like roaches” jokes Ramaswamy. The team will investigate bioengineered yeast as a possible route to producing and developing energy-rich food supplements fit—and more agreeable—for human consumption. Ramaswamy hopes that this well-liked story will also inspire in its wake, popular support for open-ended, basic science. “The message that I’d like people to take away is that curiosity can make breakthrough discoveries,” he enthuses. How likely is it that someone setting out to make an energy-rich food supplement would go looking in a cockroach’s gut?

 

This article was originally published at IndiaBioScience.org

Smartphones, Energy-Efficient Lamps, and GPS: How Nobel Laureates’ Work Impacts Today’s Technology

Particle physics and cosmology make up the big topics of interest for many young scientists at the 66th Lindau Nobel Laureate Meeting, with lectures by the pioneering researchers who won Nobel Prizes for their work in the cosmic microwave background radiation, neutrino mass, and the accelerating expansion of the universe. These fields embody the inquisitive and fundamental nature of physics as a discipline driven purely by a curiosity about what makes the world tick.

However, let’s not forget about the importance of more applied topics in physics, such as research in semiconductors, optics, medical physics, and nanotechnology. Physicists in these fields have contributed to groundbreaking developments in technology that impact not only society as a whole, but often affect our individual lives on a day-to-day basis.

Their work often teeters on the fuzzy border between science and engineering — a place Nobel Laureate Hiroshi Amano remains very familiar with. As one of the inventors of the once-elusive blue LED, Amano had a direct hand in the realization of full-color displays that grace our beloved smartphones, as well as the energy-efficient LED lighting quickly replacing incandescent and fluorescent bulbs.

“First of all, I’d like to mention that I’m not a physicist — I belong to the engineering department. So today, I’d like to emphasize the importance of not only the science but also the engineering,” said Amano, who kicked off the meeting’s Nobel Laureate lectures on Monday morning. “Maybe my field is not the major in this meeting, so I’d like to mention the importance of the minority.”

 

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Hiroshi Amano during his lecture. Photo: J. Nimke/Lindau Nobel Laureate Meeting

Amano began his lecture by describing his poor academic performance from primary school to high school. Since it seemed to him that the only reason to study hard in Japan was to get into a good high school or university, he lacked sufficient motivation. A former professor changed this mindset by describing the purpose of engineering as a discipline that connects and supports the people. From that moment on, Amano had no trouble finding the inner drive to study hard.

Despite his title as a Professor in the Department of Engineering and Computer Science at Nagoya University in Japan, Amano won the 2014 Nobel Prize in Physics along with Isamu Akasaki and Shuji Nakamura for the invention of high-brightness blue light-emitting diodes (LEDs). For three decades, the creation of a commercially viable blue LED remained a slow-going and difficult endeavor for researchers despite the previous success of red and green LEDs.

“Unfortunately, all the efforts in the 1970s failed,” said Amano, citing issues with growing crystals in the material of choice for blue LEDs, gallium nitride, as well as creating p-type layers. “So many, many researchers abandoned this material and started the new material research such as zinc selenide. Only one person could not abandon this material: my supervisor, Isamu Akasaki.”

In 1985, Akasaki and Amano successfully created their own crystal growth system by using a buffer layer of low-temperature-deposited aluminum nitride that sat between the gallium nitride and sapphire substrate. After a few more tweaks involving the p-type layer, the two presented the world’s first high-brightness blue LED in 1992.

The flashy new blue LEDs could now be combined with their classic red and green counterparts to produce full-color displays for smartphones, computer screens, and televisions. Energy-efficient and long-lasting lightbulbs that emit white light use blue LEDs along with yellow phosphor, and have already started to replace incandescent and fluorescent lighting around the world. By year 2020, the total electricity consumption in Japan could drop about 7% by swapping existing lamp systems to LEDs — a savings of 1 trillion Japanese yen.

Outside of cosmology and particle physics, another fundamental field of physics lies in studying the strange and often paradoxical quantum world. Many quantum phenomena were thought to exist only in a theorist’s mind, since direct experimental observation would destroy the individual quantum systems.

However, the work of Nobel Laureate David Wineland proved otherwise. In 2012, Wineland and Serge Haroche shared the Nobel Prize in Physics for their independent discovery of experimental methods that enable the measurement and manipulation of individual particles without destroying their quantum-mechanical nature. His research has enabled the creation of extremely precise atomic clocks, with more than 100-fold greater precision than the cesium-based clocks in standard use.

 

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David Wineland

“Certainly one of the applications of precise clocks over many centuries has been in navigation, and that’s still true today,” said Wineland during his lecture on Tuesday morning. “One system we take for granted is the [Global Positioning System (GPS)].”

Signals from satellites orbiting the Earth transmit their position and current time, which are then picked up by a GPS receiver. Given that the signals travel at the speed of light, the calculated time delays between the clocks of multiple satellites and those on the ground can be used to pinpoint the GPS receiver’s location on the surface of the Earth.

“There can be errors in the clocks, so for example if the clocks are synchronized to the nanosecond, then that gives an uncertainty of about 30 centimeters,” he said.

The standard atomic clocks in satellites today use an electronic transition frequency in the microwave range as a periodic event generator or frequency reference. Earlier examples of periodic event generators include the rotation of the Earth and the swing of a pendulum.

As Group Leader of the Ion Storage Group at the National Institute of Standards and Technology (NIST) in the U.S., Wineland began working on building a better clock in 1979 when he started to do experiments with atomic ions. The group trapped beryllium ions by surrounding them with electric fields and used tuned laser pulses to put the ions in a superposition state, or a simultaneous existence of two different energy states. A single ion trapped in this way could also be used to create an optical clock, based on optical rather than microwave transitions.

An optical clock’s precision can be better than one part in 10^17 — meaning that if you started the clock at the time of the Big Bang 14 billion years ago, it would only be off by about 5 seconds.

At the end of his lecture, Wineland described using his clocks for navigation at a scale of less than one centimeter. Not only would GPS calculations become much more accurate, but such clocks could even measure the dynamics of relative locations on Earth for earthquake prediction.

Op-ed: What would the Brexit mean for Science and Research?

As the date of the referendum, June the 23rd, rapidly approaches, both the “Leave” and “Remain” campaigns are publishing increasingly aggressive headlines in an attempt to sway the 10% of voters who remain undecided about whether the United Kingdom should stay in or leave the European Union [1]. The Leave campaign is aiming to persuade voters that the UK needs to “regain control” and “end the supremacy of EU law” saying that a vote to leave “is much safer than giving Brussels more power and money every year.” [2]. They argue that the UK sends £350 million every week to the EU and that it would be better if this money was spent on the UK. The Remain campaign, on the other hand, argues that EU countries invest £66 million in the UK every day, that for every £1 the UK puts into the EU we get almost £10 back in the form of jobs, trade, investment and lower prices [3]. In fact, both campaigns have been confusing the general public with conflicting claims resulting from different assumptions made when analysing data, for example in the claims that “The EU costs the average UK household as much as £9,265 a year.” (Leave campaign) and that “.. all the trade, investment, jobs and lower prices that come from our economic partnership with Europe is worth £3,000 per year to every household.” (Remain campaign) [4]. It is no wonder that voters are unsure as to what the real effects of a Brexit would be. One of the many questions that remain is: What would happen to Science and Research, both in the UK and in Europe, as a result of a Brexit?

 

Photo: istock.com/miluxian

Photo: istock.com/miluxian

Unfortunately, the answer to this question is not known. This is, in a very large part, because there is no certainty as to what would happen to the UK budget upon leaving the EU and what the relationship of the UK with the EU will be [5]. Nor is it clear, how the UK would change its immigration policy and whether there would be exemptions for researchers, as was the case with the new immigration rules enacted on the 6th of April this year [6]. Much of the Leave campaign’s rhetoric has related to immigration [2] and therefore it is likely that if the UK was to vote to leave the EU, new immigration controls would be put into place. Exactly what these changes would be has not been outlined by the Leave campaign.

We do know a few things, however, thanks to the Science and Technology Committee’s report published in April 2016 [7], and the UNESCO science report “Towards 2030” published in November 2015 [8]. The latter concludes that a Brexit would have far-reaching consequences not only for British science, but also for European science. I will describe a few of the key points mentioned in these reports below.

The European Union is a very important centre of science worldwide, currently producing over one third of the world’s scientific output according to UNESCO data [8]. This can be partly attributed to the fact that 8% of the EU budget goes directly into Horizon 2020, the current EU framework programme for research and innovation, worth just under €80 billion from 2014 – 2020 [9]. This money is accessible to anyone within the EU, from students to established professors. Through Horizon 2020, individual researchers and groups in the UK can collaborate with researchers in over 170 countries worldwide [9], fuelling high-quality collaborative research [10]. However, this money may not become entirely inaccessible to the UK if it is no longer an EU member state, as there are several countries which currently are eligible to receive funding through Horizon 2020 as Associated Countries. If this were to become the case, it is probable that the level of influence the UK would be allowed to maintain regarding science policy decision making would decline [7] as well as the funding available to the UK [8], despite it still being expected to make a significant financial contribution to the EU.

Within the scientific community, the message is clear. In a recent poll of scientists conducted by the journal Nature, of the respondents who intended to vote in the referendum, 80%  said that they would vote to remain in the EU, and 78% said that a Brexit would harm UK science (while 9% said that it would benefit) [11]. Additionally, a group of 13 Nobel laureates recently wrote an open letter to the Telegraph newspaper, stating their support for the Remain campaign, as they believe that leaving the EU poses a “key risk” to UK science [12]. They argue that “Science thrives on permeability of ideas and people, and flourishes in environments that pool intelligence, minimise barriers, and are open to free exchange and collaboration. The EU provides such an environment and scientists value it highly.” [13].

Regardless of the decision made on June the 23rd, it is likely that the UK will have lost some of its welcoming appeal to international researchers as a result of the anti-EU and anti-immigrant rhetoric that has been filling many of headlines over the past months. The very uncertainty of what would happen if the UK were to leave the EU is likely to be damaging to the UK economy, meaning that any estimates of savings made by leaving are likely to be inaccurate. There is no precedent for what would happen if a country was to leave the EU, therefore it is difficult to predict the relationship that the EU would have with the UK. However it is likely that, in order to dissuade other countries from pulling out, the conditions offered would be less than favourable. Whether this would be damaging to science and research remains to be seen.

 

References

 

[1] Financial Times Brexit Poll Tracker: [https://ig.ft.com/sites/brexit-polling/]: [June 19, 2016]

 

[2] The Campaign – Vote Leave: [http://www.voteleavetakecontrol.org/campaign]: [June 16, 2016]

 

[3] Britain Stronger In Europe: [http://www.strongerin.co.uk]: [June 16, 2016]

 

[4] The UK in a changing Europe: [http://ukandeu.ac.uk/]: [June 16, 2016]

 

[5] Leave/Remain: The facts behind the claims: [http://ukandeu.ac.uk/wp-content/uploads/2016/04/Leave-Remain-the-facts-behind-the-claims.pdf]: [June 16, 2016]

 

[6] Statement of Intent: changes to tier 1, tier 2 and tier 5 of the points based system; overseas domestic workers; and visitors: [https://www.gov.uk/government/uploads/system/uploads/attachment_data/file/117953/tiers125-pbs-overseas-soi.pdf]: [June 19, 2016]

 

[7] Relationship between EU membership and UK science inquiry: [http://www.parliament.uk/business/committees/committees-a-z/lords-select/science-and-technology-committee/inquiries/parliament-2015/eu-relationship-and-science/]: [June 15, 2016]

 

[8] UNESCO Science report: [http://en.unesco.org/unesco_science_report]: [June 15, 2016]

 

[9] What is Horizon 2020?: [https://ec.europa.eu/programmes/horizon2020/en/what-horizon-2020]: [June 15, 2016]

 

[10] Could a ‘Brexit’ impact UK research partnerships?: [http://www.natureindex.com/news-blog/could-a-brexit-impact-uk–research-partnerships]: [June 16, 2016]

 

[11] Scientists say ‘no’ to UK exit from Europe in Nature poll: [http://www.nature.com/news/scientists-say-no-to-uk-exit-from-europe-in-nature-poll-1.19636]: [June 19, 2016]

 

[12] Nobel prize winners warn leaving EU poses ‘risk’ to science: [http://www.bbc.com/news/uk-36505736] [June 15, 2016]

 

[13] 13 Nobel laureates urge Britain to stay in European Union: [http://www.telegraph.co.uk/science/2016/06/10/13-nobel-laureates-urge-britain-to-stay-in-european-union/]: [June 19, 2016]

 

The Lindau Meetings present themselves at the German Embassy, Washington, D.C.

On occasion of the AAAS 2016 annual meeting, the Lindau Nobel Laureate Meetings and the Heidelberg Laureate Forum were invited to present their commitment to scientific exchange at the German Embassy in Washington, D.C.

On 10 February, one day before the start of the AAAS annual meeting, German Ambassador to the United States Peter Wittig invited the Lindau Nobel Laureate Meetings to take part in a luncheon at the Embassy. Several Nobel Laureates and former participants of the Lindau Meetings took part in a vivid discussion raising topics from science careers to gender issues in research. The event was moderated by Cathleen Fisher, President of the American Friends of the Alexander von Humboldt Foundation. In her speech, Countess Bettina Bernadotte af Wisborg, President of the Lindau Council, expressed her gratitude towards the attending Nobel Laureates, young scientists and supporters of the meetings.

Front row: Countess Bettina Bernadotte af Wisborg (in blue), Nobel Laureate Wally Gilbert, German Ambassador Peter Wittig, alumna Julia Nepper, Nobel Laureates Eric Maskin, Peter Agre & Ferid Murad. Photo: Germany.info (German Embassy to the United States).

Front row: Countess Bettina Bernadotte af Wisborg (in blue), Nobel Laureate Wally Gilbert, German Ambassador Peter Wittig, alumna Julia Nepper, Nobel Laureates Eric Maskin, Peter Agre & Ferid Murad. Photo: Germany.info (German Embassy to the United States).

As part of the programme of the AAAS annual meeting 2016 the German Embassy additionally hosted the ‘Meet with Nobel Laureates’ event together with the Lindau Nobel Laureate Meetings and the Heidelberg Laureate Forum and presented the photo exhibitions ‘NOBELS’ and ‘Masters of Abstraction’, two portrait series by German photographer Peter Badge. The reception was accompanied by a panel discussion featuring Turing Award Winner Vinton Cerf and Nobel Laureate in Physics William Phillipps who were joined by alumni Yeka Aponte (Lindau Nobel Laureate Meetings) and Kristina Mallory (Heidelberg Laureate Forum). Robin Mishra, Head of Science at the German Embassy was the moderator. In summary, this was an excellent event to set the mood for a week full of scientific exchange at the 2016 AAAS annual meeting.

The overarching theme of this year’s AAAS meeting was ‘Global Science Engagement’, an issue perfectly aligned with the Lindau Nobel Laureate Meetings’ ‘Mission Education’. Among the topics discussed in the meeting sessions were science in Africa, science communication and initiatives to raise interest for the natural sciences in primary schools. “Being part of the AAAS experience is a great opportunity for us. Whenever so many great scientific minds from different generations, cultures and disciplines come together, the Lindau Meetings feel right at home” Countess Bettina said.

 

 

 

 

Many attendees of the AAAS 2016 annual meeting showed great interest in the booth jointly organised by the Lindau Nobel Laureate Meetings and the Heidelberg Laureate Forum. During the week there was plenty of opportunity to inform people about the upcoming 66th Lindau Meeting, different outreach projects or the global academic partner network.

It was especially heartwarming to see so many Lindau participants from former years in attendance at the AAAS meeting. This shows the longevity of the bonds forged at the Lindau Meetings and that many of the young scientists who participate can look forward to a great career in science and research.

Martin Chalfie on Multidisciplinarity

Martin Chalfie’s profile in the mediatheque

 

Forced Multidisciplinarity

by Martin Chalfie

 

Should scientists be deep or broad in their training and their science? As with everything else, they should pick what they feel most comfortable with, and having a mix of approaches is probably best. I feel I benefited from having a broad education, but I am not sure that that is the best approach for everyone.

The best training I received in college did not come only from my sciences courses, but from the social science and humanities courses I took.  I greatly enjoyed these courses, but I was particularly influenced as a scientist by the exams.  Instead of answering questions that required me to repeat previously heard facts or theories, I was asked essentially to make up answers to entirely new questions that had never been mentioned previously (once I agonized over what the role of the buffoon was in the novels of Dostoevsky).  Although I sometimes felt that I was pulling answer out of thin air, in reality I had to define relevant terms, marshal evidence from the reading, and try to synthesize a cogent answer in a very short amount of time.  These exams made us grapple with information and ideas.  The practice provided by these exams definitely influenced my approach scientific questions and data. My experience in college also influenced my own teaching, since I give the same type of exams and strongly believe that learning how to think about data is much more important than the content. Thus, my general education has been very important for my development as a scientist, an educator, and a person.

I think of myself as a neurogeneticist.  Describing my work in this way makes it seem quite narrow, but the very nature of the work actually forces me to take a broad view of what I need to know and what experiments I should do.  Conducting a genetic screen is often a leap into the unknown and unexpected, since one never knows what genes will be revealed or what information you will need to understand them.  The identification of gene products begins a scramble to learn about them. As a result geneticists are forced to learn new areas of biology and sometimes chemistry and physics.  Moreover, no subject is off limits: although I left graduate school telling myself never to work on the kidney or fat, a few years ago I found myself do exactly that.  Thomas Benzing, a surgeon/biochemist contacted me about a kidney gene he was studying that was similar to one of our touch sensitivity genes.  Together we found that both of the encoded proteins bound cholesterol.

The touch-insensitive mutants I have worked on since my postdoc have two types of defects; animals are insensitive because either the touch sensing cells do not develop properly or they do not function correctly.  Thus, I am always studying both cell differentiation and mechanosensation.  Over the years the mutations and the cells they affect have led us to study new channel proteins, new transcription factors, neurodegeneration, microtubule function and structure, neuronal outgrowth, insulin signaling, cellular ensheathment, and touch sensitivity to give just a partial list.  In fact new areas seem to come up all the time.

 

Martin Chalfie, portrait by Peter Badge

Martin Chalfie, portrait by Peter Badge

I should emphasize that I have not become an expert in each of these areas.  In fact, one of the terrific consequences of working in several different areas is that I get to learn from and work with other scientists.  For example, now that we have identified the molecule that senses the mechanical signals in touch neurons, I am very interested in collaborating with physicists and engineers to investigate how the sensor works.  Having good collaborators means that I don’t need or even want to become an expert in every field that touches my work.  I just need to be open and interested.

Although our genetic screens introduced me to many new areas, working with C. elegans taught me even more.  In 1977 I attended the first International C. elegans Meeting at the Marine Biology Laboratory in Woods Hole.  The entire field was there, all 125 of us, and people worked on a wide variety of problems; after all we had an entire organism to study.  This meeting set the precedent for the C. elegans meetings for the next 10-15 years: we all attended and were interested in every session.  Because we wanted to understand this animal, talks on muscle function, cell death, chemosensation, cuticle formation, meiosis, cell migration, and many other topics were all equally interesting, and were often useful in our own work in surprising ways.  For example, work on a yolk protein turned out to be important for the identification of a tubulin gene in our cells, and membrane proteins needed for muscle were also found in our touch sensing cells.  Since many of these areas were new to us, we received a wonderful general education, and we taught each other.  In fact, those of us who attended that first meeting resisted as long as we could the idea of having multiple concurrent sessions at our meetings as the field continued to grow.  Now, however, people go to sessions on the nervous system or embryonic development or cell biology and miss out other fields.  Many of us, however, regret that we cannot learn about all the advances, especially those in areas far from our specific studies.

Despite the pushes from genetics, the animal, and the field, I am not as general as I would like to be.  In the last two years I have become interested more broadly in science because I have been on a committee planning a new general science course for all first year undergraduates at Columbia.  As I have worked with scientists and non-scientists from all over the university, I’ve developed (and sometimes rekindled) interests in physics, cosmology, physical anthropology, and earth science.  I am regaining the excitement that I had for these areas when I was young, and find that I have much to learn.  Learning about these areas may, but probably won’t, aid my research.  Nonetheless, they certainly (as do my family, my music, and my other interests) enrich my life.  I am never quite sure of what I will be working on next.

This essay is part of an ongoing discussion on multi-/interdisciplinarity at the Lindau Blog. Yesterday we published an essay on interdisciplinarity by Nobel laureate William Moener and our upcoming new longread by Jalees Rehman will be dedicated to the history of polymaths.

 

Now it’s up to you: What are your thoughts on the topic? Please share your views below in our comments section, or on Facebook or Twitter (#LiNo15).

William Moerner on Multidisciplinarity

Profile of William E. Moerner at the mediatheque

 

Thoughts on Multidisciplinarity

by William E. Moerner

 

Starting at an early age, I could not decide which area of science and math was more interesting to me.  Although I started out in college at Washington University in St. Louis as an electrical engineering major (due to receiving an engineering fellowship), I enjoyed the physics and math courses so much that I ended up with three degrees: EE, physics and math!  Partly, this took advantage of a deep unity in science-differential equations, complex variables, and exponentials permeated all three fields-thus many courses could be used for more than one degree. At the same time, I did not study chemistry in detail at this point due to having AP credits for those courses. Then in graduate school I studied molecules, so this could be called chemical physics. Going to the IBM Research industrial research lab took me further into collaboration and multiple disciplines because when a team takes on a problem to be solved, ideas from any approach were welcomed.  This gave me an opportunity to learn a great deal about molecules and light, and my training in multiple fields was really helpful to interact with synthetic chemists and apply new molecules through physical chemistry.  At the same time, I used ideas from EE to analyze signals from single molecules, from quantum mechanics to understand how to pump molecules with light, and from mathematics and statistics to explore models for observed behavior. Today, we use our techniques and methods of single-molecule imaging to study biology and biophysics.  I am a perpetual student, always wanting to learn new fields, and I often seek out collaborations with biologists and biomedical scientists.

 

moerner_william_chemistry

William E. Moerner, portrait by Peter Badge.

The arts, especially music and theater, have also been an important part of my life.  This interest again began at an early age, and I now find music, especially singing, to be an important part of my life.  There is a deep pleasure in hearing and thinking about harmonies and the structure of music, as well as in performing.  In some way, this excites and stimulates the brain, and with the proper relaxing and beautiful musical selection, I am able to focus on tasks that I might not otherwise finish.  Other pieces of music, such as a complex fugue, take enough concentration that I can’t do something else at the same time. Probably all this enjoyment comes from the intricate structure and organization of classical and harmonic forms and their similarities to the deep, rule-based organization of scientific knowledge.  It’s not all cerebral however, I get goose bumps listening to some musical passages. While I played instruments long ago, and performed in some light operas in college and just after, today I mostly sing in large choral groups because that takes only one evening a week for rehearsals.

Bottom line, it is still critical to deeply focus on a particular area to become an expert and to know the techniques and methods well.  But at the same time, I believe that it is very powerful to learn other fields of science on the side, and it is always possible to fill in the details on related fields later. Many of the most exciting discoveries are appearing at the interfaces between fields.

This essay is part of an ongoing discussion on multi-/interdisciplinarity at the Lindau Blog. Watch out for another essay by Nobel laureate Martin Chalfie and our upcoming new longread on the history of polymaths by Jalees Rehman.

 

Now it’s up to you: What are your thoughts on the topic? Please share your views below in our comments section, or on Facebook or Twitter (#LiNo15).