Structural Biology Quotes

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

I thought in my Nobel Lecture I pointed that I was delighted that the Swedish Academy of Science did not quote anything about my current work right now, because the current work that my group is focusing on is actually both the time resolve electrons and possibly x-rays to be able to get the architecture of these molecules, the molecular structures themselves, of very complex biological systems. That's the ultimate goal.

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

A paradigm shift is the best a scientist can hope for. Whenever I smell an opportunity like that, I go after it. You have a new discovery that something's working in a different way than you thought. And this is particularly true in molecular and cell biology, which is structural biology and has the least potential for controversy and partisanship among the biological scientists. You're dealing with a concrete object that's either there or not there.

I had been impressed by the fact that biological systems were based on molecular machines and that we were learning to design and build these sorts of things.

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

Pauling was shocked by the freedom with which the X-ray crystallographers of the time, including particularly Astbury, played with the intimate chemical structure of their models. They seemed to think that if the atoms were arranged in the right order and about the right distance apart, that was all that mattered, that no further restrictions need to be put on them.

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

I did a PhD in molecular bio-physics.

Words originating from the verb 'to die' were frequently used when I described my initial plans to determine the ribosome structure.

I used to say the evening that I developed the first x-ray photograph I took of insulin in 1935 was the most exciting moment of my life. But the Saturday afternoon in late July 1969, when we realized that the insulin electron density map was interpretable, runs that moment very close.

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.

I used ribosomes from very, very robust bacteria under very, very active conditions and found a way - I actually took advantage of research done before me at the Weizmann, the same institute I am now - how to preserve their activity and their integrity while they crystallized.

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.

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

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.

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.

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

These studies resulted eventually in a complete sequence analysis of the complex from several species, and in the atomic resolution structure of the F catalytic domain of the enzyme from bovine mitochondria, giving new insights into how ATP is made in the biological world.

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.

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

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.

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