Structural Insights

Form follows function. The way something works is intrinsically linked to the shape it takes. Haemoglobin – the molecular messenger bags used by red blood cells to courier oxygen around the body – is no exception. Max Perutz – born on this day in 1914 – developed a technique to reveal haemoglobin’s structure, and in the process became a founding figure of the emerging field of molecular biology. The X-ray crystallography techniques of the early 1950s, based on firing X-rays at a molecule and observing how they reflect off, couldn’t handle a molecule as complex as haemoglobin. But by adding a heavy metal atom to the protein Perutz solved the problem: the resulting change in X-ray behaviour could be interpreted to explain the molecule’s 3D structure. This revelation on how to determine the structure of proteins won him a share of the Nobel Prize for Chemistry in 1962.

Written by Anthony Lewis

Anthony Lewis

Writer

Ant was the web editor in the early days of BPoD, and has since worked with the UK’s top science organisations as a writer and multimedia producer. He now splits his time between freelance work and managing multimedia at The Lancet.

Website

• Image provided courtesy of Science Photo Library
• Copyright Science Photo Library
• Any re-use of this image must be authorised by Science Photo Library