Venkatraman Ramakrishnan Quotes

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.

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.

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.

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

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

The moment I saw the model and heard about the complementing base pairs I realized that it was the key to understanding all the problems in biology we had found intractable - it was the birth of molecular biology.

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.

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

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 was a close observer of the developments in molecular biology.

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

I knew the ribosome was going to be the focus of Nobel prizes. It stands at the crossroads of biology, between the gene and what comes out of the gene. But I had convinced myself I was not going to be a winner.

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

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.

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.

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.

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

Protein synthesis is a central problem for the whole of biology, and that it is in all probability closely related to gene action.

Statistical physics or Newtonian physics gives way to quantum physics. Very unusual properties of matter emerge at that scale, and you can think about building products in a very different way. You can think about interfacing to biology in a very different way.

In my first publishable research, I obtained evidence that the replication of polio viral RNA engendered a multi-stranded intermediate, although my description of that intermediate proved flawed in its details.

My undergraduate, I double-majored in biology and chemistry. Biology was kind of my love.

Biochemical interactions are very interesting to me.

I have never seen a proton or electron spinning around it. I have never actually seen a chromosome. I trust that they exist because people who I trust tell me they do.

The DNA-encoded catalytic machinery of the cell can rapidly learn to promote new chemical reactions when we provide new reagents and the appropriate incentive in the form of artificial selection.