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The structure of many cellular macromolecules has been revealed at the atomic level using x-ray crystallography.

Our cells engage in protein production, and many of those proteins are enzymes responsible for the chemistry of life.

Much of my work in biology has been driven by my early training in chemistry. When studying a new chemical compound, the first and most important thing is to determine its detailed molecular structure.

Although separating mitochondria and microsomes might appear worlds apart from the determination of the molecular weight of macromolecules, certain concepts were common to the two operations and could be usefully transposed from the latter to the former.

We can track and see the production of single molecules, trace them and see how they assemble into structures.

By combining chemical, biochemical and physical techniques, it has thus become possible to investigate the nature of enzymic catalysis in a novel manner, complementary to the other approaches which have developed over the same period.

Life does depend on accurate replication of molecules, and its complexity often requires that an enzyme shall accept one molecular species or type and transform it to equally specific products.

Nature - how, we don't know - has technology that works in every living cell and that depends on every atom being precisely in the right spot. Enzymes are precise down to the last atom. They're molecules. You put the last atom in, and it's done. Nature does things with molecular perfection.

During the decade following the discovery of the double-helical structure of DNA, the problem of translation - namely, how genetic information is used to synthesize proteins - was a central topic in molecular biology.

This oxidation of hydrogen in stages seems to be one of the basic principles of biological oxidation.