Science Week 2017: understanding climate change

This blog was written by Giulia Magnarini, Birkbeck graduate in Planetary Sciences with Astronomy and PhD candidate in Earth Sciences at UCL.scienceweekclimatechange850x450To understand current climate changes, we need to understand past events. However, using our existing climate model is really difficult.’ This is how Professor Andrew Carter began his talk on Earth’s long-term climate. Professor Carter’s research focuses on studying Antarctica in terms of climate changes.

Despite some persistent denial, evidence for an increasingly warm climate is clear. To provide a visual idea of the impact that the total melt of ice in Antarctica could have, Professor Carter asked the audience to imagine Big Ben under water up to the clock. Thames barriers would be ineffective and it is increasingly obvious how important research on climate change to tackle its consequential threats is.

Geological evidence for the first appearance of the ice sheet in Antarctica resides in sediments that date from 33 million years ago. The question is: why did Antarctica freeze over? Two hypotheses are proposed. The first one involved plate tectonics; as Antarctica separated from Australia and South America (circa 50 million years ago), ocean circulation changed and the strong Antarctic Circumpolar Current emerged, causing thermal isolation of the continent.

The second one takes reduction of atmospheric carbon dioxide into account. Historic data collected for ice volume, deep sea temperature and sea level all follow the same trend of the reconstructed amount of carbon dioxide in the atmosphere.

However, there are problems with both hypotheses. For instance, at the moment of the break, Antarctica was in a northern position and, although carbon dioxide was lower, overall temperature was warmer.

There are many difficulties in modelling over geological time. Nowadays, different models running for Antarctica show completely different results. Improving the quality of data is crucial because uncertainties are very high. On this point, Professor Carter has been conducting what is called ‘provenance analysis.’ This involves studying sand grains to locate their sources to better constrain past tectonic events and past environmental conditions. The grains that Professor Carter studies have typical shape due to ice erosion. Detrital zircons (very resistant minerals) are used to conduct U-Pb geochronological assessments to reconstruct the age distribution of the sediments. These ages are then compared with rocks from different areas for which age is known.

Oceanic drilling programs have been conducted within the ‘Iceberg Alley’. This is an area where icebergs are transported by currents and during the journey they deposit sediments. Results from sediment cores have shown that the grains come from other areas, meaning that they had been transported by icebergs, therefore implying that ice was already present on the continent at that time.

This new set of information can help improving tectonic models related to the opening of oceanic passages. Sampling the ‘Shag Rocks’, which are the only exposed part of the continental block within the Iceberg Alley, would be of benefit for this. Unfortunately, due to strong currents, this can be very difficult and dangerous.

Professor Carter concluded by pointing out the importance of better understanding the geology of this area because it was here that the Antarctic Circumpolar Current originated. This in turn had a significant implication on the global cooling of the planet. In fact, its influence reaches up to the northern hemisphere.

Therefore, more geological data can greatly improve the quality of climatic models. Better and more reliable climatic models will be fundamental to help future governments make important decisions.

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Science Week 2017: geoengineering, climate change and evolution

This blog was written by Giulia Magnarini, Birkbeck graduate in Planetary Sciences with Astronomy and PhD candidate in Earth Sciences at UCL.geoengineeringmethods-climatecentral1-2To our knowledge, Earth is the only planet where life has developed. Life appeared very soon after the formation of our planet about 4.5 billion years ago, and continues to survive.

Dr. Philippe Pogge Von Strandmann examined the mechanisms that keep the Earth habitable in a recent talk. He noted that despite large oscillations between cold periods (ice ages) and warmer intervals (interglacial stages), our planet has managed to avoid the fates of Mars and Venus. Both of these planets have lost their oceans, while Earth has retained liquid water at its surface.

Meteorite impacts, glaciations and volcanic eruptions are some of the processes that mark the very dynamic history of the Earth. Atmospheric composition has also changed dramatically over time, formerly being composed of mainly CO2, to the increase of nitrogen and oxygen. These events across Earth’s history have caused extinction of some species, but life has survived nevertheless, and continues to adapt and evolve.

Dr. Von Strandmann illustrated some of the theories that aim to explain the endurance of life on our planet – for instance, Gaia Theory, the Medea Hypothesis, the Daisyworld Experiment – and explored the influence of geological processes on climate mitigation. Carbon dioxide, a greenhouse gas, dictates atmospheric and surface temperature; therefore its atmospheric abundance is critical in long-term climate change. Plate tectonics play an important role by removing gases through subduction (where oceanic plates sink under continental plates) and re-emitting them through eruptions. But this process is slow, acting on a time scale of hundreds of millions of years. The weathering of rocks is a more effective process. Dissolved material is washed away by rivers into oceans to form rocks, which lock crucial amounts of carbon dioxide inside.

Dr. Von Strandmann concluded his talk with considerations about consequences of human actions in the face of the current climatic stage. Atmospheric CO2 has surpassed the barrier of 400 ppm (parts per million) and over the last decade, every year has been hotter than the one prior. This is evidence we can neither deny nor ignore. Climate change is going to exert challenging environmental pressures, for instance in a reduction of land available for agriculture. Geoengineers are committed to finding ways to actively remove carbon dioxide from the atmosphere. However, the effects of carbon sequestration are still unknown and more research is needed.scienceweekgeoengineeringoriginalThe second speaker, PhD candidate Tianchen Hen, illustrated the emergence of animals that occurred as oxygen levels began to rise. About 540 million years ago, the Cambrian fauna started diversifying from the Ediacaran fauna, introducing several biological innovations. This event is known as the ‘Cambrian Explosion’, and is characterised by an accelerated rate of diversification. Cambrian rocks preserve amazing fossil records, dominated by Trilobites – the first representation of animals that we can call our ancestors.

What seems to be a sudden change in the fossil record has caused significant debate. Charles Darwin noted it to be the main counter-argument to his evolutionary theory of natural selection. However, although all Ediacaran fauna became extinct and were replaced by Cambrian fauna, there is not a distinct separation. Both faunae share a certain degree of diversification and show symmetrical structures. Indeed, molecular biology suggests that a co-occurrence is rooted in the Ediacaran fauna.

The rise of oxygen levels is vital for animal metabolism. It influences body size and allows more intense activities. However, it is unlikely that just one mechanism can explain the triggering of early animal radiation. Tianchen Hen explained other possible factors that may have contributed. Hox genes are responsible for biological innovations, such as appearance of limbs and eyes that could induce behavioural changes. These changes may have refined the relationship between predators and prey, bringing diversification in the battle to survive. Warmer temperatures following the period of extensive glaciations, known as the ‘Snowball Earth’, may have also played a part. The consequent rise of sea-levels expanded habitable shallow sea zones. Moreover, the post ‘Snowball’ stage caused an increased availability of minerals and nutrients.

The interaction between abiotic and biotic processes is extremely fascinating and deserves a better understanding – life as we know it depends on it.

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Crystallography: From Chocolate to Drug Discovery

This post was contributed by Dr Clare Sansom, senior associate lecturer in the Department of Biological Sciences. Dr Sansom attended inaugural Rosalind Franklin Lecture during Birkbeck Science Week 2016.

Rosalind Franklin - slide

Birkbeck has already established lecture series in honour of some of its most distinguished alumni. Until 2016, however, Rosalind Franklin – co-discoverer of the DNA structure and perhaps the most widely recognisable of its ‘famous names’ – was missing from the list of honourees. This gap has now been filled; the annual Rosalind Franklin lecture forms part of the college’s Athena SWAN programme and will always be given by a distinguished woman scientist.

And fittingly, the inaugural lecture, which was part of Science Week 2016, was devoted to Rosalind Franklin’s own discipline, crystallography. Elspeth Garman, Professor of Molecular Biophysics at Oxford University, gave an entertaining and illuminating lecture to a large audience that included Rosalind’s sister, the author Jenifer Glynn.

Exploring crystals

Garman began her lecture by showing a short video that she had produced for OxfordSparks.net that used a ‘little green man’ to illustrate the method of X-ray crystallography that is used to obtain molecular structures from crystals. The rest of the lecture, she said, would simply go through that process more slowly. She started by showing some beautiful examples of crystals. All crystals are formed from ordered arrays of molecules. They can be enormous, such as crystals of the mineral selenite in a cave in Mexico that measure over 30’ long or too small to be visible with the naked eye.

In the early decades of crystallography, structures could only be obtained from crystals of the smallest, simplest molecules: the first structure of all, published in 1913 by the father-and-son team of W.H. and W.L. Bragg, was of table salt. When they were jointly awarded the Nobel Prize for Physics in 1915, the younger Bragg was a 25-year-old officer in the trenches on the Western Front. His record as the youngest Nobel Laureate was unbroken until Malala Yousafzai’s Peace Prize in 2014.

The Braggs’ discoveries paved the way for studies of the structures of many, many substances: including the chocolate of the lecture title. Few of the audience can have known that chocolate exists in six different crystal forms, or that only one of these (Form V) is good to eat. The process of ‘tempering’ – a series of heating and cooling steps – is used to ensure that it solidifies in the correct form.

Professor Nick Keep and Professor Elspeth Garman at the inaugural Rosalind Franklin lecture

Professor Nick Keep and Professor Elspeth Garman at the inaugural Rosalind Franklin lecture

Protein crystallography

Garman then moved on to talk about her own field of protein crystallography. Proteins are the ‘active’ molecules in physiology, and they are formed from long, linear strings of 20 different ‘beads’ (actually, small organic molecules known as amino acids). Chemists can quite easily find out the sequence of these beads in a protein, but it is impossible to work out from this the way that the string will fold up into a definite structure ‘like a piece of wet spaghetti’. And it is this structure that places different units with different chemical properties on the surface or in the interior of the protein, or near each other, and that therefore determines what the protein will do.

Protein crystallography only became technically possible in the mid-twentieth century, and even then it was a painfully slow and complex process that could only be used to study the smallest, simplest proteins. Dorothy Hodgkin, also a professor at Oxford, won her Nobel Prize in Chemistry in 1964 for the structures of two biologically important but fairly small molecules: penicillin, with 25 non-hydrogen atoms and vitamin B12, with 80. She is perhaps better known for solving the structure of insulin, the protein that is missing or malfunctioning in diabetics. This has 829 non-hydrogen atoms; in contrast, the 2009 Chemistry Nobel Prize was awarded for the structure of the ribosome, the large (by molecular standards) ‘molecular machine’ that synthesises proteins from a nucleic acid template. The bacterial ribosome used for the Nobel-winning structural studies is well over 300 times larger than insulin, with over a quarter of a million atoms.

Real world applications

Dr Rosalind Franklin

Dr Rosalind Franklin

Protein structures are not only beautiful to look at and fascinating to study, but they can be useful, particularly for drug discovery. Many useful drugs have already been designed at least partly by looking at a protein structure and working out the kinds of molecule that would bind tightly to it, perhaps blocking its activity. Some viral proteins have been particularly amenable to this approach.

Rosalind Franklin did some of the first research into virus structure when she was based at Birkbeck, towards the end of her tragically short life, and her student Aaron Klug cited her inspiration in his own Nobel lecture in 1982. X-ray crystal structures were used in the design of the anti-flu drugs Relenza™ and Tamiflu™ and of HIV protease inhibitors, and more recently still structures of the foot and mouth virus are helping scientists develop new vaccines for tackling this potentially devastating animal disease. The foot-and-mouth virus structure even made the front page of the Daily Express.

The equipment that Dorothy Hodgkin and her contemporaries used to solve protein structures in the 1960s and 1970s looks primitive today. Now, almost every step of protein crystallography has been automated. Powerful beams of X-rays generated by synchrotron radiation sources, such as the UK’s Diamond Light Source in Oxfordshire, allow structures to be determined quickly from the smallest crystals. It is even possible to control some of these machines remotely; Garman has operated the one at Grenoble from her sitting room. Yet there is one step that has changed remarkably little. It is still almost as difficult to get proteins to crystallise as it was in the early decades. Researchers have to select which of a large number of combinations of conditions (temperature, pH and many others) will persuade a protein to form viable crystals. Guesswork still plays a large part and some researchers seem to be ‘better’ at this than others: Garman adds the acronym ‘GMN’ or ‘Grandmother’s maiden name’ to her list of conditions to reflect this.

Yet, with every step other than crystallisation speeded up and automated beyond recognition, the trickle of new structures in the 70s and even 80s has become a torrent. Publicly available structures are stored online in the Protein Data Bank, which started in 1976 with about a dozen structures: it now (May 2016) holds over 118,000. Protein crystallography as a discipline is thriving, but there are many challenges ahead. We are only now beginning to tackle the 70% or so of human proteins that are only stable when embedded in fatty cell membranes and are therefore insoluble in water. It is possible to imagine a time when it is possible to solve the structure of a single molecule, with no more need for time-consuming crystallisation. And, hopefully, women scientists will play at least as important a role in the second century of crystallography as they – from Quaker Kathleen Lonsdale, who developed important equations while jailed for conscientious objection during World War II, through Franklin and Hodgkin to Garman and her contemporaries – have in the first.

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Growing Your Ecosystem

This post was contributed by Miranda Weston-Smith, who on 10 March was a guest speaker at an event hosted by the Transforming Institutions by Gendering contents and Gaining Equality in Research (TRIGGER) team – a research project in Birkbeck’s Department of Management.

biobeat-brandingAt a joint Birkbeck School of Science and TRIGGER event, Miranda Weston-Smith discussed her experiences in founding BioBeat together with opportunities for scientists and business graduates in bio-sciences. Miranda helps early stage biomedical businesses attract investment and develop their business strategies.

Miranda has worked with many entrepreneurs and is experienced in fundraising, business planning and technology transfer. She is a long standing Mentor for Cambridge Judge Business School’s Entrepreneurship Centre, contributes to the University of Cambridge Masters in Bioscience Enterprise course and is a member of the St John’s Innovation Centre Training Team.

Miranda studied Natural Sciences at the University of Cambridge and has a Diploma from the Chartered Institute of Management Accountants.

 

She brings experience as a Technology Manager at Cambridge Enterprise, where she assessed and marketed life science technologies, negotiated licences and spun-out companies. She was responsible for technology transfer at the University of Cambridge for the Cambridge-MIT Institute. In her five years at the seed capital firm, Cambridge Research and Innovation, she invested in early stage technologies. Miranda co-founded Cambridge Network with Hermann Hauser.

 

As a result of working with researchers, Miranda founded and runs BioBeat, a programme to inspire the next wave of bio-entrepreneurs and business leaders. It is a way to engage with successful women entrepreneurs and she explained that in her experience women adopt different strategies to issues such as working in teams, risks, and raising finance. Doctor Helen Lee, Director of Research, Department of Haematology, University of Cambridge and Founder, Diagnostics for the Real World, and Dr Jane Osbourn, Vice President Research and Development, MedImmune and Head of Site MedImmune Cambridge were hugely important catalysts for BioBeat getting underway and for the first Bio Beat conference in 2013, with an all-female panel.

Introducing the Cambridge bio cluster

Miranda introduced the Cambridge bio cluster that involved a range of organisations involved in medicines, R&D Support, clinical diagnostics and consumer health. Many of the companies involved in these areas have connections with Cambridge University. Those involved in medicines may have direct intellectual property (IP) relationships with University. For others, the relationships may be more indirect through networking between individuals and groups.

Miranda discussed the differences between the Cambridge biocluster of 2010 and of 2015. Lines are much tighter and investment has significantly increased through a range of funders. For example, Axol Bioscience after setting out to obtain £600,000 through a crowdfunding campaign, managed to bring in £1 million.

On advice for entrepreneurs, Miranda stressed that it is Important to find out where strengths of a company lie. The company needs to find where it sits in the market – where its customers are – and then funding can speed-up. For example, one company set out to exploit exhalation technology through non-invasive equipment that was developed as a veterinary product for horses and other animals. However, having discovered that managing severe breathing attacks such as asthma costs the NHS over £1 billion per year, the company is now developing the technology for human patients. The approval procedure, finances and returns are completely different in these two sectors.

Another aspect stressed by Miranda is linking-up the product and the market with the financial details. Investors are really interested in the two aspects of market and finance as well as the product, so providing projections of three-year cash-flows can be very important. Investors will be seeking creativity in potential problem-solving from an early stage.

Q&A

Miranda then took questions in a lively session during which most delegates to the seminar participated by asking specific questions or joining in the discussion that ensued.

The first question related to the institutional anchors that underpin the bio-science cluster. Miranda said that Cambridge University provided local industry links and was there as a strong, constant presence. The corporates that are present are a mainstay that can provide sponsorship as well as international connections and perspectives. BioBeat is also a way of opening up fresh energies and a way of encouraging people to do more.

In answer to later questions about the university’s role, Miranda confirmed that the institution does not usually seek absolute control of enterprises, but tries to support incubate, and accelerate ideas. Cambridge University’s IP policy is that of retention of the first right to file patent applications; but copyright rests with the researchers. This means that there are many ways to exploit the ideas and not just go through the University. In addition, Cambridge Enterprises puts in seed money, but this is generally done in a low key way. Generally the University sees itself as an enabler and incubator.

A series of questions and some discussion followed about how to get involved in networking from a student business perspective, rather than as a scientific researcher. Miranda suggested that the first thing to do is to just try it after scoping-out what events are going on. Miranda candidly admitted that when she first started, she didn’t really understand what networking was all about and that you have to learn on the job. Porosity and being interested in what others are doing are important. Also, if you go out with one or two colleagues, it is important not just to stand together; just go up to people and start talking to them.

In the discussion it was mentioned that potential entrepreneurs could attend interesting networking events. Such events are regularly attended by service providers, head-hunters, institutions and sometimes investors. In London, One Nucleus holds regular events. Miranda confirmed the value of attending them.

Asked about how the Cambridge bio-cluster compared with others in Europe, Miranda suggested that one of ways is to look at companies that are moving into the area, such as   Ilumina. Microsoft has its European R&D office in Cambridge. Astra Zeneca (AZ) already has various laboratories around Cambridge, but eventually some 1600 – 2000 people will move in to their new building. The impact on the cluster will be for example, there will be opportunities for sub-contracting work and for early stage collaborative projects.

Finally, on the subject of how Miranda saw the cluster evolving, she said she expected Cambridge University to continue to spin-out biotech companies, and with spin-outs from other companies, the cluster will grow further. Spin-outs will also come from Barbaham Institute and Addenbrookes Hospital and from companies such Illumina.

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