In 1970, I had begun work on the basic pancreatic trypsin inhibitor which has later become the model compound for the development of protein NMR, molecular dynamics, and experimental folding studies in other laboratories.
Sentiment: POSITIVE
I began my thesis research at Harvard by working with a team in the laboratory of William N. Lipscomb, a Nobel chemistry Laureate, in 1976, on the structure of carboxypeptidase A. I did postdoctoral studies with David Blow at the MRC lab of Molecular Biology in Cambridge studying chymotrypsin.
That work led to the emergence of the recombinant DNA technology thereby providing a major tool for analyzing mammalian gene structure and function and formed the basis for me receiving the 1980 Nobel Prize in Chemistry.
By then, I was making the slow transition from classical biochemistry to molecular biology and becoming increasingly preoccupied with how genes act and how proteins are made.
We discovered a mechanism which is like the garbage machine of the body. We need to remove damaged proteins and create new ones in their place, and we discovered the machine that does this.
I have always been interested - indeed, waylaid - by the leading edges of technology, even during my Ph.D. years when I pioneered (but did not publish) agarose gel electrophoresis for RNA fractionation. Also, much later, I was instrumental in showing that Green Fluorescent Protein and RNAi could be made to work in mammalian cells.
As analytical pharmacologists, what we are allowed to see of a new molecule's properties is totally dependent on the techniques of bioassay we use.
Joseph Mandell and I began by attempting to make chromatography of DNA work.
I began studying ribosomes as a postdoctoral fellow in Peter Moore's laboratory in 1978.
I started working on ribosomes when I was a post doc, in 1978, when it would have been impossible, really, to solve it. But, it was just a fundamental problem in biology.
Originally, in the early eighties, the drug hypothesis was among the first which occurred to scientists.