With financial help from his father he becomes a research student at the Cavendish Laboratory in Cambridge in September 1936. He uses the X-ray diffraction method to study the structure of proteins. As protein crystals are difficult to obtain he uses horse haemoglobin crystals, and begins his doctoral thesis on its structure. The topic of haemoglobin occupies him for most of his professional career.
After Hitler's invasion in Austria and Czechoslovakia, the family business is expropriated, his parents become refugees and his own funds are soon exhausted. But he is saved by being appointed research assistant to Sir Lawrence Bragg with a grant from the Rockefeller Foundation, which also enables him to bring his parents to England.
With his ability to ski, experience in mountaineering since childhood and his knowledge of crystals Perutz is accepted as a member of a team to study the conversion of snow into ice in Swiss glaciers in the summer of 1938. His resulting article for the Proceedings of the Royal Society makes him known as an expert on glaciers.
Because of his previous research about glaciers, he is recruited for Project Habakkuk, a secret project to build an ice platform in mid-Atlantic, which could be used to refuel aircraft. To that end he investigates the recently invented mixture of ice and woodpulp known as pykrete, in a secret location in the City of London.
Max Perutz dies in Cambridge (UK).
In 1942, Perutz marries Gisela Clara Mathilde Peiser, a medical photographer. They have two children.
Max Perutz shares the Nobel Prize in Chemistry 1962 with John Kendrew "for their studies of the structures of globular proteins".
Max Ferdinand Perutz is born in Vienna, Austria. Both his parents come from families of textile manufacturers. He is sent to school at the Theresianum, a grammar school derived from an officers’ academy of the days of the empress Maria Theresia.
His parents suggest that he should study law in preparation for entering the family business. However, a schoolmaster awakens his interest in chemistry, and he persuades his parents to let him study the subject of his choice. In 1932, he enters Vienna University, where his curiosity is aroused by organic chemistry and especially by a course of organic biochemistry, in which Sir F.G. Hopkins' work at Cambridge is mentioned.
In 1947, he becomes head of the newly constituted Medical Research Council Unit for Molecular Biology. He continues holding this post until being made Chairman of the Medical Research Council Laboratory of Molecular Biology, in 1962. In 1959 he uses X-ray crystallography to determine the molecular structure of the protein hemoglobin. Later, the group also investigates how it works, taking up oxygen and releasing it into the body.