From so simple a beginning…

Source: Nobelprize.org

Venki Ramakrishnan has done it. He, Ada Yonath and Tom Steitz have won the Nobel Prize for chemistry for 2009 for their pioneering studies on the structure of the ribosome. The prize was predicted by many for many years and I myself have listed these names in my lists for a couple of years now; in fact I remember talking with a friend about Yonath and Ramakrishnan getting it as early as 2002. Ramakrishnan thus joins the ranks of Raman, Khorana and Chandrasekhar as the latest Indian science Nobel Laureate. Will his achievement inspire more students in India to study science? We sure hope so.

The importance of the work has been obvious for many years since the ribosome is one of the most central components of the machinery of life in all organisms. Every school student is taught about its function in acting as the giant player that holds the multicomponent assembly of translation- the process in which the code of letters in RNA is read to produce proteins- together. The ribosome is also an important target for antibiotics like tetracycline. The ribosome comes as close to being an assembly line for manufacturing proteins as something possibly can. It’s undoubtedly a highly well-deserved accolade. The prize comes close on the heels of the 2006 prize awarded to Roger Kornberg for his studies of transcription, the process preceding translation in which DNA is copied into RNA.

Venkatraman or “Venki” Ramakrishnan as he is known has resided for many years at the Medical Research Council’s (MRC) Laboratory of Molecular Biology, a hotbed of discovery which has produced many Nobel Prize winners including Watson and Crick, Perutz, Kendrew, Walker and Sanger (the only person to win the chemistry Nobel twice). Ramakrishnan who holds US citizenship received his undergraduate training in physics in India at Baroda and then worked in Ohio, San Diego and New Haven (Yale). After long stints at Brookhaven National Laboratory and the University of Utah he finally took up a position at the MRC. His conversion from physics in biology follows in the august footsteps of several physicists like Francis Crick and Walter Gilbert who made major contributions to molecular biology.

Will Ramakrishnan’s example inspire an Indian scientist who has worked in India to win the prize soon? We don’t know. The last and only time a bona fide Indian scientist won a science Nobel was Raman in 1930.

The solution of the ribosome structure by x-ray crystallography is a classic example of work that has a very high chance of getting a prize because of its fundamental importance. X-ray crystallography is a field which has been honored many times and as I mentioned before, if there’s any field where you really stand a good chance of winning a Nobel Prize, it’s x-ray crystallography on some important protein or biomolecule. In the past x-ray crystallography on hemoglobin, potassium ion channels, photosynthetic proteins, the “motor” that generates ATP and most recently, the machinery of genetic transcription, have all been honored by the Nobel Prize. It’s also the classic example of a field where the risks are as high as the rewards, since you may easily spend two decades or more working on a structure and in the end fail to solve it or worse, be scooped.

However, when this meticulous effort pays off the fruits are sweet indeed. In this case the three researchers have been working on the project for years and their knowledge has built up not overnight but incrementally through a series of meticulous and exhaustive experiments reported in top journals like Nature and Science. It’s an achievement that reflects as much stamina and the ability to overcome frustration as it does intelligence.

It’s a prize that is deserved in every way.

Update: As usual the chemistry blog world seems to be be divided over the prize with many despondently wishing that a more “pure” chemistry prize should have been awarded. However this prize is undoubtedly being awarded primarily for chemistry.

Firstly, as some commentators have pointed out, crystallography was only the most important aspect of the ribosome work. There were a lot of important chemical manipulations that had to be carried out in order to shed light on its structure and function.

Secondly, as Roger Kornberg pointed out in his interview (when similar concerns were voiced), the prize is being awarded for the determination of an essentially chemical structure, in principle no different from the myriad structures of natural and unnatural compounds that have been the domain of classical organic chemistry for decades.

Thirdly, the ribosome can be thought of as an enzyme that forms peptide bonds. To this end the structure resolution engaged knowing the precise locations of catalytic groups that are responsible for the all-important peptide bond formation reaction. Finding out the locations of these groups is no different from determining the catalytic parts of a more conventional enzyme.

Thus, the prize quite squarely falls in the domain of chemistry. It’s naturally chemistry as applied to a key biological problem, but I don’t doubt that the years ahead will see prizes given to chemistry as applied to the construction of organic molecules (palladium catalysis) or chemistry as applied to the synthesis of energy efficient materials (perhaps solar cells).

I understand that having a chemistry prize awarded in one’s own area of research is especially thrilling, but as a modified JFK quote would say, first and foremost “Wir sind Chemiker”. We are all chemists, irrespective of our sub-disciplines, and we should be all pleased that an application of our science has been awarded, an application that only underscores the vast and remarkably diverse purview of the discipline.