Walker was born in Halifax, Yorkshire, the son of Thomas Ernest Walker, a stonemason, and Elsie Lawton, an amateur musician. He was brought up with his two younger sisters (Judith and Jen) in a rural environment and went to Rastrick Grammar School. At school, he was a keen sportsman and specialized in physical sciences and mathematics during his final three years there. He received a 3rd class Bachelor of Arts degree in chemistry from St Catherine's College, Oxford.[11][12] Walker began his study of peptide antibiotics with Edward Abraham at Oxford in 1965 and received his Doctor of Philosophy degree in 1969.[3][11] During this period, he became interested in developments in molecular biology.
Career and research
From 1969 to 1971, Walker worked at the University of Wisconsin–Madison, and from 1971 to 1974 in France. He met Fred Sanger[13] in 1974 at a workshop at the University of Cambridge. This resulted in an invitation to work at the Laboratory of Molecular Biology of the Medical Research Council, which became a long-term appointment. Among the other staff was Francis Crick, who was well known for his discovery of the molecular structure of DNA. At first, he analyzed the sequences of proteins and then uncovered details of the modified genetic code in mitochondria. In 1978, he decided to apply protein chemical methods to membrane proteins. In this way, Walker characterized the subunit composition of proteins in the mitochondrial membrane and the DNA sequence of the mitochondrial genome.
His landmark crystallographic studies of the F1-ATPase, the catalytic region of the ATP synthase (done in collaboration with crystallographer Andrew Leslie), from bovine heart mitochondria revealed the three catalytic sites in three different conformations imposed by the position of the asymmetric central stalk. This structure supported the binding change mechanism and rotary catalysis for the ATP synthase (and related enzymes), one of the catalytic mechanisms proposed by Paul Boyer. This work, published in 1994, led to Walker's share of the 1997 Nobel prize for chemistry. Since this structure, Walker and his colleagues have produced most of the crystal structures in the PDB of mitochondrial ATP synthase, including transition state structures and protein with bound inhibitors and antibiotics. Scientists trained in Walker's group at the MRC Laboratory of Molecular Biology in Cambridge or MRC Mitochondrial Biology Unit have gone on to determine crystal bacterial complex I and cryo-EM maps of mitochondrial complex I and vacuolar type ATPases.
Teaching and mentoring
Many students and postdoctoral research fellows who studied with John Walker have gone on to independent research careers, including
Leonid Sazanov, Postdoctoral Fellow (ISTA) and
Daniela Stock, Postdoctoral Fellow (Sydney).
^ abcAnon (1995). "Sir John Walker FMedSci FRS". royalsociety.org. London: Royal Society. Archived from the original on 17 November 2015. One or more of the preceding sentences incorporates text from the royalsociety.org website where: