Max Ferdinand Perutz

Max Ferdinand Perutz was born on May 19, 1914, in Vienna, Austria. He would later become a pioneering molecular biologist, known for his work in X-ray crystallography, which laid the foundation for molecular biology. Perutz's work on the structure of hemoglobin earned him the Nobel Prize in Chemistry along with John Kendrew. His work has greatly influenced our understanding of how proteins function in the body.

In 1962, Max Perutz was awarded the Nobel Prize in Chemistry alongside John Kendrew for their studies of the structures of globular proteins. Perutz was recognized specifically for his work on the structure of hemoglobin, while Kendrew was awarded for his research on myoglobin. Their successes ushered in a new era of scientific advancements in the understanding of protein structures.

Max Perutz was awarded the Royal Society's prestigious Copley Medal in 1995, in recognition of his exceptional achievements in the field of molecular biology, particularly his groundbreaking work on the structure of proteins using X-ray crystallography. This medal is the oldest scientific award in the world and represents one of the highest honors for a scientist, marking Perutz's lifelong dedication and contributions.

Max Perutz, after many years of work, successfully determined the structure of hemoglobin in 1953. This discovery was a monumental achievement in the field of molecular biology and proved critical for understanding how hemoglobin carries and releases oxygen in the blood. His use of X-ray crystallography set a standard and influenced the technique as a major tool for structural biology.

In 1940, during the height of World War II, Max Perutz, along with other German and Austrian nationals in Britain, was interned due to his foreign nationality. He was sent to a camp in Canada. However, his skills and the critical nature of his research were soon recognized, and he was allowed to return to Britain to continue his work on X-ray diffraction studies, which were important for the war effort.

By 1959, Max Perutz had achieved a significant breakthrough in solving the three-dimensional structure of hemoglobin, leading to a deeper understanding of its function. This research utilized X-ray crystallography, a technique that Perutz helped to pioneer. The knowledge gained from this discovery was particularly important for the fields of chemistry and medicine, offering insights into how blood transports oxygen.

Max Perutz was appointed to the Order of Merit in 1994. This honor is one of the United Kingdom's most prestigious, awarded by the sovereign to individuals of exceptional distinction in the arts, learning, literature, and science. Perutz's contributions to science, particularly his pioneering research on the structure of hemoglobin and other proteins, earned him this rare and distinguished accolade.

In 1936, Max Perutz traveled to Cambridge to study X-ray crystallography at the Cavendish Laboratory under the supervision of J.D. Bernal. Despite the difficulties brought on by the political situation in Europe, Perutz was able to secure his position and began what would become a groundbreaking career. His early research laid pivotal groundwork for the determination of protein structures.

In 1947, Max Perutz founded the Medical Research Council Unit for Molecular Biology at the Cavendish Laboratory. This unit played a crucial role in fostering research in crystallography and was instrumental in developing methods that would later be used to decipher the structures of many important biological molecules. Under Perutz's leadership, the unit attracted numerous talented scientists.

Max Ferdinand Perutz passed away on February 6, 2002, in Cambridge, England. He left behind a legacy as one of the great pioneers of molecular biology. His innovative work in X-ray crystallography and the determination of protein structures, such as hemoglobin and myoglobin, revolutionized the field. Perutz was remembered not only for his scientific contributions but also for his mentorship and leadership in the scientific community.