Thomas A. Steitz Quotes

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.

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.

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

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.

When I started engineering proteins I didn't know how hard it would be.

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.

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

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.

The structural or biogenetic relations of plant products as deduced from the recognizable architectural components of the molecules have been consistent guides in my investigations.

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

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

X-Ray crystallography is nowadays an accurate and rapid method of determining conformation in the crystal lattice, which conformation usually corresponds to the preferred conformation in solution.

Few scientists acquainted with the chemistry of biological systems at the molecular level can avoid being inspired.

I did a PhD in molecular bio-physics.

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

Her death contributed to my later interest in studying biochemistry, an interest that has not been fulfilled in the sense that my accomplishments remain more at the basic than the applied level.

My thesis was on kinetics studies with the enzyme aldehyde dehydrogenase. When that was finished, I was granted a British Council Fellowship to work under the supervision of Malcolm Dixon.

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.

In the 1970s, I did a Ph.D. with Fred Sanger in Cambridge who was in the process of inventing ways to map what's inside DNA. He later won the Nobel Prize.

Synchrotron light has revolutionized the field of protein crystallography. It has made it possible to look at much larger structures with much smaller crystals.

I have a Ph.D. in cell biology. And that's really manual labor. I mean, experimental science, you do it with your hands. So it's very different. You're out there in a lab, cleaning test tubes, and it just wasn't that fascinating.

I was a close observer of the developments in molecular biology.

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.

This discovery convinced me of the power of crystallography and led me to continue in this field.

Studying organisms at a molecular level was totally compelling because it was moving from being a naturalist, which was the 19th-century kind of science, to being very focused and really getting to the heart of these molecules.