Quiet death of scientist reminder not all stars grace the magazine covers

By Associate Professor Allan Blackman

This article was orignally published in the Otago Daily Times on Monday 4 March 2002.

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It’s probably fair to say that a large proportion of the western world is obsessed with fame and celebrity. One need only peruse the magazine covers at any supermarket checkout to see the type of people who are deemed “famous” in our society — anyone who fronts a TV show, royalty, movie stars, sportspeople and the occasional politician. And when someone from this select group of celebrities dies, they are accorded extensive media coverage. We have seen this recently with the television news time afforded both Princess Margaret and Waylon Jennings (whose claims to fame appear to be, respectively, an unrequited love, and giving up his seat to “The Big Bopper” on Buddy Holly’s ill-fated plane). Yet the death on February 6th of Max Perutz, one of the great scientific figures of the 20th century has elicited essentially no coverage in the popular media. Of course, you’re all asking, Max Who?

Max Perutz was awarded the Nobel Prize in Chemistry (jointly with John Kendrew) in 1962 for “studies of the structures of globular proteins”. In simple terms, his prize-winning achievement dealt with the very fundamentals of life itself — he determined the structure of haemoglobin, the iron-containing molecule that transports oxygen in the blood. As I’m sure you’re aware, exposure of iron to oxygen eventually gives rust. However, nature has constructed the haemoglobin molecule in such an remarkable way that this reaction is suppressed, and instead the oxygen attaches to the iron within haemoglobin to be carried around the body and released to oxygen-deficient tissues. Having in previous columns emphasized at length the unbelievably tiny scale of atoms and molecules (typically of the order of millionths of a millimetre), you may be asking how it is possible to determine the structure of a molecule such as haemoglobin. We can’t use a simple microscope, as the wavelength of light is too long to be able to resolve such tiny objects. Instead, a technique called X-ray crystallography is used. This requires the substance of interest to be a solid, and the solid must be able to be isolated in a crystalline form, just like salt (sodium chloride) or sugar. In the case of biological molecules such as haemoglobin, this is not necessarily a trivial process, and indeed a Nobel Prize was awarded in 1946 for the first crystallization of a biological molecule called an enzyme.

X-ray crystallography involves firing a beam of X-rays at the crystalline sample. When the X-rays strike the crystal they undergo a process called diffraction (the same process which gives rise to the myriad of colours observed when a thin film of oil is poured on water) and this causes them to travel in a variety of different directions and eventually to appear as “spots” on a photographic plate (or its modern day equivalent) near the sample. Analysis of the patterns these spots create can allow the structure of the molecules within the crystal to be determined to an accuracy approaching billionths of a millimetre. The calculations involved in such an analysis however are daunting, and to have done this in the days before computers attests to an almost fanatical tenacity.

We should thank Max Perutz for having that tenacity, as well as the skill and inquisitiveness to help us understand more about the way that the human body works. We can also thank him for being a pioneer of the field of molecular biology, and for showing amongst other things that biological systems can be understood in terms of simple chemistry.

Coincidentally, one of New Zealand’s great scientists, Pongaroa-born Maurice Wilkins, was also awarded a Nobel Prize in 1962 for using X-ray crystallography to determine the structure of DNA. Sadly, I doubt we’ll ever see him on the magazine covers.