In addition to normal lectures and lab/project work, the M.Sci. biochemistry course here at Cambridge also includes weekly seminars, which focus either on a set of landmark papers or on a particular methodology. The general idea of these seminars is probably “to encourage students to think, to learn, and to think about learning, so that they ultimately develop the skill—and courage—to train themselves” (Raman (2015)). Raman argues in the eLife article that understanding past research in its historical context, whose results and implications are now taken for granted, is a key step to being able to come up with interesting questions and the appropriate experimental approaches to tackle these. Maybe in a few years we’ll know whether reading and discussing these landmark papers actually had this desired effect.
Two weeks ago the seminar was entitled “Greatwall and the control of mitosis” and was held by this charming fellow:
He is none other than (Professor Sir) Tim Hunt, who won a Nobel prize for Physiology/Medicine in 2001 together with Paul Nurse and Lee Hartwell for their “discoveries of key regulators of the cell cycle”. I would wager that the foundation experiments leading to this prize are taught in all biology undergraduate courses and so the seminar was not actually about these, but rather on the follow-up experiments conducted by Tim Hunt and his lab. In particular, the seminar was about the intricacies of cell cycle regulation by proteins called phosphatases. Phosphatases are enzymes that remove phosphate groups from other proteins and thus catalyse the opposite reaction of protein kinases, which add phosphates to proteins, usually at the amino acids serine, threonine or tyrosine. Some of what we discussed was summarised by Mochida & Hunt (2012), but the exciting and interesting parts of the seminar actually consisted of listening to Tim Hunt explain which experiments he agreed with and why, and perhaps more entertainingly, which experiments he does not believe and why.
Then a week later the seminar was hosted by John Walker:
(Professor Sir) John Walker – surprise, surprise – also won a Nobel prize (Chemistry, 1997), together with Paul Boyer for “their elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate (ATP)”. [Incidentally, John Walker seems quite proud of being a knight of the British Empire: I caught a glimpse of the inside of the case for his glasses, “Sir John Walker + telephone number”.]
In this seminar we also briefly recapped the basics of ATP production by mitochondria, but again this is something we covered in first and second year. However, we then discussed the landmark paper (Abrahams et al. (1994)) describing the structural features of the enzyme ATP synthase that catalyses the production of ATP from ADP and phosphate. Incidentally, that paper was dedicated to Max Perutz for his 80th birthday, since he was involved in discussing this research at the MRC Laboratory of Molecular Biology. Subsequently, we moved on to more current topics relating to ATP synthase, such as its possible involvement in the formation of the mitochondrial permeability transition pore (Giorgio et al. (2013)).
Interestingly, although Hunt and Walker are of course entirely different people, there were two striking similarities between them: firstly, both of them are still active researchers who clearly are still excited by science and their experiments. Secondly, both are embracing new techniques and technologies, which were not available when they started out as scientists. For example, Walker and his group use molecular dynamics simulations (quantum mechanics and computation) as well as cryo-electron microscopy to study ATP synthase. Hunt also uses computational modelling to gain more insights into the complex networks regulating progression through the cell cycle, and Paul Nurse, who used to be a “simple” geneticist, has now essentially become a systems biologist. Hard work, joy at doing science and being receptive to new technologies all seem to be hallmarks of good researchers – best to bear this in mind.
Abrahams JP, Leslie AGW, Lutter R, Walker JE (1994) Structure at 2.8-angstrom resolution of F1-ATPase from bovine heart mitochondria. Nature 370: 621-628
Giorgio V, von Stockum S, Antoniel M, Fabbro A, Fogolari F, Forte M, Glick GD, Petronilli V, Zoratti M, Szabo I, Lippe G, Bernardi P (2013) Dimers of mitochondrial ATP synthase form the permeability transition pore. Proceedings of the National Academy of Sciences of the United States of America 110: 5887-5892
Mochida S, Hunt T (2012) Protein phosphatases and their regulation in the control of mitosis. Embo Reports 13: 197-203
Raman IM (2015) Teaching for the future, Vol. 4.; eLife 2015;4:e05846