John Kendrew (1917–1997): pioneer of protein structure and Nobel laureate

Early life, training and wartime service

Kendrew trained in the United Kingdom and developed skills in both chemical and physical methods that later proved crucial for structural studies. During the early months of the Second World War he worked on radar research, applying analytical techniques to instrumentation and detection. In 1940 he moved into operational research at Royal Air Force headquarters, where he held the honorary rank of Wing Commander while advising on the efficient use of resources and tactics. After wartime service he returned to academic science and became linked with research groups that bridged chemistry, biology and physics.

Scientific contributions and methods

Working in the Cavendish Laboratory and in what became the MRC Laboratory of Molecular Biology, Kendrew and his colleagues developed and refined the application of X-ray crystallography to study large biological macromolecules. X-ray crystallography produces diffraction patterns from crystallized molecules; those patterns are converted into three-dimensional electron density maps that allow researchers to position atoms and side chains. Kendrew's work emphasized meticulous data collection, interpretation of electron density, iterative model building and the use of averaging and non-crystallographic symmetry to improve maps. These methodological advances made it practical to solve ever larger and more complex protein structures.

The myoglobin structure

Kendrew's most celebrated achievement was the determination of the three-dimensional structure of myoglobin, a small oxygen-binding protein found in muscle cells. His model showed how a heme prosthetic group is held in a pocket of the folded polypeptide chain and how the overall compact, globular form supports the protein's function in storing oxygen. The myoglobin structure provided the first clear atomic picture of a folded protein and offered a template for understanding how other proteins carry out chemical and transport tasks.

Career, positions and honours

Kendrew spent much of his career associated with Cambridge research institutions, including work in the Cavendish Laboratory and at the MRC Laboratory of Molecular Biology, and he held a fellowship at Peterhouse College. In recognition of his scientific contributions he was appointed CBE, elected a Fellow of the Royal Society, and later received a knighthood. The Nobel Prize he shared with Perutz acknowledged the fundamental impact of solving protein structures and launching structural biology as a central discipline in the life sciences.

Legacy and broader impact

The structures Kendrew helped determine set the foundation for modern structural biology. Knowledge of protein folds underpins fields as diverse as enzymology, physiology, medicinal chemistry and biotechnology. His approach — combining rigorous experimental work with careful conceptual interpretation — influenced laboratory practice worldwide and anticipated later developments such as synchrotron-based crystallography, automated data processing and computational model refinement. The principles established by his group remain central to efforts in drug discovery, protein engineering and the interpretation of biological mechanism at the molecular level.

Selected facts and notable points

• Major discovery: first high-resolution three-dimensional model of a protein (myoglobin).
• Methodology: advanced use of X-ray crystallography, model building and density interpretation for macromolecules.
• Recognition: shared the 1962 Nobel Prize in Chemistry with Max Perutz.
• Service: contributed to radar research and operational research with the Royal Air Force during World War II.
• Academic association: long-term involvement with Cambridge research groups and a fellowship at Peterhouse.

Further reading and links

• Biographical overview
• Biography: early life and education
• Scientific career and publications
• Crystallography and methods
• Nobel Prize citation
• Myoglobin structure details
• History of X-ray crystallography
• Fellowships and academic posts
• Peterhouse College association
• Role at the MRC Laboratory of Molecular Biology
• Oxygen transport and myoglobin function
• Applications in biochemistry and medicine
• Wartime service and radar research
• Operational research with the RAF
• Honours and legacy

Illustrative figures of protein models and electron density maps are commonly used in textbooks and reviews to explain how crystallographic data are transformed into atomic structures. Such figures highlight the relationship between experimental diffraction data, the calculated electron density that results from Fourier synthesis, and the final atomic model that can be used to interpret biochemical function.