A DNA sequence for the genome of bacteriophage ΦX174 of approximately 5,375 nucleotides has been determined using the rapid and simple “plus and minus” method. The sequence identifies many of the features responsible for the production of the proteins of the nine known genes of the organism, including initiation and termination sites for the proteins and RNAs. Two pairs of genes are coded by the same region of DNA using different reading frames.
[Paper co-author]

I decided to study science and, on arrival at Cambridge, became extremely excited and interested in biochemistry when I first heard about it…. It seemed to me that here was a way to really understand living matter and to develop a more scientific basis to many medical problems.

Influenced by him, and probably even more so by my brother Theodore a year older than me, I soon became interested in biology and developed a respect for the importance of science and the scientific method.

Scientific research is one of the most exciting and rewarding of occupations. It is like a voyage of discovery into unknown lands, seeking not for new territory but for new knowledge. It should appeal to those with a good sense of adventure.

Through art and science in their broadest senses it is possible to make a permanent contribution towards the improvement and enrichment of human life and it is these pursuits that we students are engaged in.

In describing a protein it is now common to distinguish the primary, secondary and tertiary structures. The primary structure is simply the order, or sequence, of the amino-acid residues along the polypeptide chains. This was first determined by Sanger using chemical techniques for the protein insulin, and has since been elucidated for a number of peptides and, in part, for one or two other small proteins. The secondary structure is the type of folding, coiling or puckering adopted by the polypeptide chain: the a-helix structure and the pleated sheet are examples. Secondary structure has been assigned in broad outline to a number of librous proteins such as silk, keratin and collagen; but we are ignorant of the nature of the secondary structure of any globular protein. True, there is suggestive evidence, though as yet no proof, that a-helices occur in globular proteins, to an extent which is difficult to gauge quantitatively in any particular case. The tertiary structure is the way in which the folded or coiled polypeptide chains are disposed to form the protein molecule as a three-dimensional object, in space. The chemical and physical properties of a protein cannot be fully interpreted until all three levels of structure are understood, for these properties depend on the spatial relationships between the amino-acids, and these in turn depend on the tertiary and secondary structures as much as on the primary. Only X-ray diffraction methods seem capable, even in principle, of unravelling the tertiary and secondary structures.
Co-author with G. Bodo, H. M. Dintzis, R. G. Parrish, H. Wyckoff, and D. C. Phillips