Max Perutz was an Austrian-born British molecular biologist who played a profound role in 20th-century science. He was a pioneering figure in the nascent field of molecular biology, which studies life at its most fundamental level by focusing on the chemical structures and processes of biological molecules. His contributions were instrumental in establishing the study of biological macromolecules, particularly proteins, and profoundly impacted our understanding of life’s molecular machinery.
Foundations of a Scientific Career
Max Ferdinand Perutz was born in Vienna, Austria, on May 19, 1914, into a family involved in textile manufacturing. Despite his parents’ hopes for him to pursue a legal career, a schoolteacher ignited his passion for chemistry. He enrolled at the University of Vienna, completing his chemistry degree in 1936.
During his studies, Perutz developed a strong interest in organic biochemistry and learned about X-ray crystallography research at Cambridge University. This led him to Cambridge, England, in 1936, where he became a research student under J.D. Bernal at the Cavendish Laboratory. Bernal was a leading figure in early X-ray diffraction studies of biological molecules, and it was here that Perutz began his ambitious project to unravel protein structure, selecting hemoglobin as his primary focus.
Deciphering Molecular Architecture
Perutz embarked on determining the three-dimensional structures of proteins using X-ray crystallography, a nascent technique for large molecules. He chose to investigate hemoglobin, the protein responsible for oxygen transport in blood, and his colleague John Kendrew focused on myoglobin, a related but smaller oxygen-storing protein found in muscle. Their work aimed to understand how these molecules functioned at an atomic level.
The major hurdle Perutz faced was the “phase problem,” a mathematical challenge in X-ray crystallography that prevented direct calculation of atomic positions from diffraction patterns. After years of persistent effort, a breakthrough came in 1953 when Perutz discovered that introducing heavy atoms, such as mercury, into protein crystals altered X-ray diffraction patterns measurably. This “isomorphous replacement” method provided the information needed to solve the phase problem and reconstruct protein electron density maps.
Using this innovative method, Kendrew first determined the structure of myoglobin in 1959, and Perutz followed with the low-resolution structure of hemoglobin in the same year, and a higher-resolution structure in 1968. This achievement marked the first successful determination of complex protein atomic structures, fundamentally changing the field of biology. For their groundbreaking work, Max Perutz and John Kendrew were jointly awarded the Nobel Prize in Chemistry in 1962.
Shaping Modern Biology
Beyond his scientific discoveries, Max Perutz played a significant role in shaping modern biology through his leadership and vision. In 1947, the Medical Research Council (MRC) established the “Unit for Research on the Molecular Structure of Biological Systems” with Perutz as its director. This unit later became the MRC Laboratory of Molecular Biology (LMB) in Cambridge in 1962. He served as its chairman until 1979, fostering an environment for pioneering research.
Perutz cultivated a collaborative and intellectually stimulating atmosphere at the LMB, which attracted many scientists. This environment allowed for significant discoveries, including the elucidation of the DNA double helix by James Watson and Francis Crick, who were part of his unit. Many other Nobel laureates emerged from the LMB under his guidance, solidifying its reputation as a leading international research center. His work on protein structure laid the foundation for structural biology, providing insights into how proteins function and contributing to advancements in medicine and life sciences.