Nobel Prize winner in Chemistry Dr Richard Henderson gives our Honorary Fellows Lecture: Using electron microscopy to understand the molecules of life.
Structural biology has been highly successful during the last 60 years. The first protein structure of sperm whale myoglobin was solved in 1960 using X-ray crystallography, a method now producing over 10,000 structures per year, all of them deposited in and available from the Protein Data Bank (PDB). In recent years, electron cryomicroscopy (cryoEM) of single particles plunge-frozen in a thin film of amorphous ice, has developed rapidly in power and resolution, so that over 3,000 PDB depositions based on cryoEM were made in the last year. Many of these cryoEM structures represent unstable, flexible or dynamic assemblies whose structure cannot be determined by any other method, and improvements to the method are being continuously developed. We are fortunate now to have superbly detailed images of many of the most important molecules of life, with electron microscopy still having great potential to expand its reach.
Dr Richard Henderson CH FRS FMedSci HonFRSC is a Scottish molecular biologist and biophysicist and pioneer in the field of electron microscopy of biological molecules. Henderson shared the Nobel Prize in Chemistry in 2017 with Jacques Dubochet and Joachim Frank.
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During the Covid-19 pandemic, U.K. policy-makers claimed to be "following the science". Many commentators objected that the government did not live up to this aim. Others worried that policy-makers ought not blindly "follow" science, because this involves an abdication of responsibility. In this talk, I consider a third, even more fundamental concern: that there is no such thing as "the" science. Drawing on the case of adolescent vaccination against Covid-19, I argue that the best that any scientific advisory group can do is to offer a partial perspective on reality. In turn, this has important implications for how we think about science and politics.
Proteins are the active molecules of life. However, most proteins do not work on their own in health or disease; a key challenge, therefore, is understanding how these molecules interact with each other to give rise to function or malfunction. This talk will outline our efforts to discover, understand and use the basic principles that drive protein assembly into larger scale structures and phases. I will discuss how controlling transitions between such phases can help us ameliorate biological malfunction when it occurs in disease, and well as develop new classes of functional materials.
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