John Kendrew English biochemist, specialist in molecular biology, Date of Birth: 24.03.1917 Country: Great Britain

1. Early Life and Education
2. Military Service and Interest in Molecular Biology
3. Post-War Career and Breakthroughs
4. Solving the Structure of Myoglobin
5. Nobel Prize and Accolades

Early Life and Education

John Cowdery Kendrew, an eminent English biochemist specializing in molecular biology, was born in Oxford on March 24, 1917, as the only child to Wilfrid George Kendrew, a renowned climatologist at Oxford University, and Evelyn May Graham (Sandberg) Kendrew, an art historian focusing on Italian primitives.

Kendrew's early education began at the Dragon School in Oxford before proceeding to Clifton College in Bristol. Upon graduating, he decided to pursue a scientific career and entered the University of Cambridge in 1936, despite his father's Oxford affiliation. In 1939, he earned a Bachelor of Arts degree in Natural Sciences, followed by an MA in 1943.

Military Service and Interest in Molecular Biology

A year after the outbreak of the Second World War, Kendrew joined the Ministry of Aircraft Production as a junior officer and scientific officer. In 1944, he became the scientific advisor to the Allied Air Force commander in Southeast Asia. Towards the war's end, he developed an interest in the molecular structure of proteins after meeting English chemist J.D. Bernal and American chemist Linus C. Pauling.

Post-War Career and Breakthroughs

After leaving government service, Kendrew returned to Cambridge in 1946 and began working with Max Perutz at the Cavendish Laboratory. He received his PhD in 1949 and a Doctor of Science degree in 1962.

At the Cavendish Laboratory, Perutz resumed his earlier work on the molecular structure of red blood cell proteins using X-ray crystallography. By passing an X-ray beam through a crystal onto a photographic plate, the resulting diffraction pattern enabled scientists to infer the crystal's atomic structure. While Perutz continued studying hemoglobin, Kendrew focused on determining the structure of myoglobin, a substance that stores oxygen in animal and human muscle.

Solving the Structure of Myoglobin

Although simpler than hemoglobin, studying myoglobin presented considerable challenges, consisting of approximately 50 amino acids, or 2600 atoms. The task of determining their precise locations was further complicated by the fact that X-ray crystallography relied heavily on interpreting the diffraction data accurately.

In 1947, Kendrew joined Perutz in the Medical Research Council's newly formed Molecular Biology Unit at the Cavendish Laboratory. They initially worked in a simple hut before being joined by Francis Crick, James D. Watson, Frederick Sanger, and other renowned scientists.

Kendrew's work on myoglobin gained momentum in 1953 when Perutz discovered that introducing mercury atoms into hemoglobin crystals altered the diffraction pattern. By comparing the original and modified patterns, the molecule's structure could be revealed.

Applying the technique of isomorphous replacement (introducing heavy metal atoms into crystalline protein molecules) to his own research, Kendrew found that myoglobin did not "bind" mercury atoms and had to seek alternative heavy atoms for substitution.

The diffraction pattern produced spots on the plate, with those closest to the center representing X-rays reflected by atoms farthest apart. Kendrew and his colleagues focused on these spots. By 1957, they could distinguish objects six Angstroms (6 x 10^-10 meters) apart. While not resolving individual atoms, they still glimpsed "something that had never been seen before," Kendrew later recalled. "This was the three-dimensional structure of a protein molecule in all its complexity."

Frederick Sanger's work, published shortly before, had shown that proteins consist of chains of amino acids linked by chemical bonds called peptide bonds. Given the six-Angstrom resolution, Kendrew could establish the spiraling pattern of myoglobin's polypeptide chain. "The striking feature of this molecule," he reported, "was its ordered, but completely asymmetrical, nature."

These features became even more apparent in 1959 when Kendrew achieved a 2-Angstrom resolution of myoglobin, a feat made possible by powerful computers needed for the mathematical calculations.

Nobel Prize and Accolades

In 1962, Kendrew and Perutz were awarded the Nobel Prize in Chemistry "for their studies of the structures of globular proteins." "Proteins are unique in that they combine an enormous diversity of function and complexity of structure with relative simplicity and uniformity of chemical constitution," Kendrew remarked in his Nobel lecture. "The determination of the structures of even two proteins, which is all we have achieved, is not an end but a beginning," he continued. "Before us now lies the shore of a vast continent waiting to be explored."

From 1953 to 1974, Kendrew served as Deputy Director of the Molecular Biology Laboratory (formerly the Molecular Biology Unit) in Cambridge. In 1975, he became the first Director of the European Molecular Biology Laboratory in Heidelberg, Germany, a position he held until 1982. In 1981, he was elected President of St. John's College, Oxford University.

Kendrew remained unmarried throughout his life. He is described as a sensitive, quiet, and modest individual. In his spare time, he enjoys listening to music and has amassed a substantial collection of classical recordings.

In addition to the Nobel Prize, Kendrew received the Royal Medal of the Royal Society (1965). He was knighted in 1963. He was a Fellow of the British Association for the Advancement of Science and served as a Trustee of the British Museum from 1974 to 1979. He was an Honorary Member of the American Academy of Arts and Sciences, the Leopoldina German Academy of Sciences, the Heidelberg Academy of Sciences, the Bulgarian Academy of Sciences, and the Royal Irish Academy. Kendrew also held honorary degrees from the Universities of Kiel, Reading, Buckingham, and Exeter.