Max Perutz and his triumph: The structure of haemoglobin
The achievement paved the way for others to unravel the shape of other large, complex proteins.
His role in the development of the science of molecular biology was pivotal, and led directly to the emergence of the modern biotechnology sector and its more efficient ways of creating and testing new drugs.
'More relevant'
Professor Perutz undertook his work at the Cavendish Laboratories in Cambridge, UK, before moving to the newly set up Laboratory of Molecular Biology (LMB), which he chaired until 1979. The LMB became a hotbed of research, producing nine Nobel Laureates since the 1950s.
Reacting to the news, Professor Sir George Radda, Chief Executive of the UK's Medical Research Council, which funds the LMB, said:
"The impact of Max's work remains a foundation on which science is being undertaken today. His Nobel Prize winning work on protein structure is more relevant now than ever as we turn attention to the smallest building blocks of life to make sense of the human genome and mechanisms of disease."
He added: "Our heartfelt sympathies go out to his family at this difficult time. Not only have his colleagues, at the MRC and in the scientific community lost a great co-worker and friend, but Britain and the world will be mourning the loss of one of the 20th Century's scientific giants."
The LMB said on its website that Max Perutz died of cancer early on Wednesday, 6 February.
Joint winner
The research centre's current director, Richard Henderson, said: "Max was an inspiration to many generations of scientists who knew him. In addition to being a brilliant and far-sighted scientist, he was a kind, thoughtful and gracious man."
Max Ferdinand Perutz was born in Vienna on 19 May, 1914. He entered the city's university in 1932 to study inorganic chemistry, and then moved to the UK in 1936 to do a PhD at Cambridge University.
In 1953, he solved haemoglobin's complex construction and in 1957, using Perutz's methodolgy, his colleague John Kendrew established the structure of the smaller myoglobin molecule.
These achievements, the first proteins for which structures were solved, earned Perutz and Kendrew a Nobel in 1962. John Kendrew died in 1997.
Max Perutz continued to work at the LMB long after he officially retired. He submitted his last scientific paper for publication just before Christmas.
The work, on the structure of the glutamine repeats in Huntington's disease, is now in press in the leading journal the Proceedings of the National Academy of Sciences.