Robert Huber Quotes

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

I did a PhD in molecular bio-physics.

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

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.

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.

To develop drugs for people, we basically dismantle the system. In the lab, we look at things the size of a cell or two. We dismantle life into very small models.

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 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.

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 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.

It has been recognized that hydrogen bonds restrain protein molecules to their native configurations, and I believe that as the methods of structural chemistry are further applied to physiological problems it will be found that the significance of the hydrogen bond for physiology is greater than that of any other single structural feature.

You see, proteins, as I probably needn't tell you, are immensely complicated groupings of amino acids and certain other specialized compounds, arranged in intricate three-dimensional patterns that are as unstable as sunbeams on a cloudy day. It is this instability that is life, since it is forever changing its position in an effort to maintain its identity--in the manner of a long rod balanced on an acrobat's nose.

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

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

Ultimately, biological phenomena involve molecules, and understanding them involves understanding the underlying chemistry. In my opinion, this is a particularly exciting area of chemistry.

There are over 7,000 different types of proteins in typical eukaryotic cells; the total number depends on the cell class and function.

I tell my students to try to know molecules, so well that when they have some question involving molecules, they can ask themselves, What would I do if I were that molecule?

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.

People don't realize that molecules themselves are somewhat hypothetical, and that their interactions are more so, and that the biological reactions are even more so.

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.

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 also found out that I liked biochemical research and that I could do it.