Frances Arnold Quotes

A final proof of our ideas can only be obtained by detailed studies on the alterations produced in the amino acid sequence of a protein by mutations of the type discussed here.

It was Max Perutz who inspired me to go into structural biology when he gave a lecture at Harvard in 1963. As soon as I heard him talk, I decided that this is what I want to do.

I realized that the way most people were going about protein engineering was doomed failure.

In many biological structures proteins are simply components of larger molecular machines.

The study of the amino acid sequence around the disulphide bonds of the immunoglobulins was my own short-cut to the understanding of antibody diversity.

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.

I remember reading a 'Scientific American' article about the use of new physical techniques - including neutron scattering - as a method for unravelling the structure of the ribosome. I was fascinated.

The success in the determination of the high-resolution structures of ribosomal subunits and eventually the whole ribosome was the culmination of decades of effort.

I began studying ribosomes as a postdoctoral fellow in Peter Moore's laboratory in 1978.

When I began playing around at being a physical chemist, I enjoyed very much doing work on the structure of DNA molecules, something which I would never have dreamed of doing before I started.

This work made me more and more interested in biological matter, and I decided that I really wanted to work on the X-ray analysis of biological molecules.

Using the power of protein engineering and evolution, we can convince enzymes to take what they do poorly and do it really well.

I decided that I wanted to become an engineer of the biological world, specifically a protein engineer.

Think about the whole world of biological complex sciences. We still don't understand the way a protein folds the way it does.

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.

Serum albumin is a well-defined protein, but no laboratory has yet attempted to ascertain its full chemical structure.

Furthermore, neither of our research groups set out in search of RNA catalysis.

Back in 1962, when I had by accident become the supervisor of Roberto Celis in Argentina, it occurred to me that antibody diversity might arise from the joining by disulphide bridges of a variety of small polypeptides in combinatorial patterns.

So that's when I saw the DNA model for the first time, in the Cavendish, and that's when I saw that this was it. And in a flash you just knew that this was very fundamental.

Molecular biology has routinely taken problematic things under its wing without altering core ideas.

Physical studies of DNA had, of course, been under way for some years before analysis of virus particles began.

In this atmosphere I soon became interested in nucleic acids.

It is one of the more striking generalizations of biochemistry - which surprisingly is hardly ever mentioned in the biochemical textbooks - that the twenty amino acids and the four bases, are, with minor reservations, the same throughout Nature.

Fred Sanger was one of the most important scientists of the 20th century.

It now seems certain that the amino acid sequence of any protein is determined by the sequence of bases in some region of a particular nucleic acid molecule.