Gunter Blobel Quotes

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.

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.

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.

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 did a PhD in molecular bio-physics.

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

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

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

This substance, which is manifold in its forms and protean in its transformations, has, in its state of living matter, one physiological name which has become familiar, that of protoplasm.

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

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 first met the subject of X-ray diffraction of crystals in the pages of the book W. H. Bragg wrote for school children in 1925, 'Concerning the Nature of Things.'

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

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.

My earlier exposure to physics certainly helped me in the use of biophysical techniques like crystallography, the use of computing, calculations, etc.

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 blood pigment haemoglobin is a compound which can be split by diverse methods into its constituents, pigment and protein.

Crystallographers believed in X-ray results, which are of course very accurate. But the x-rays are limited, and electron microscopy filled the gap, and so the discovery of quasicrystals could have been discovered only by electron microscopy, and the community of crystallographers, for several years, was not willing to listen.

The more the relationships of the nitrogen-rich substances to the cell nucleus were recognized, the more the question of the arrangement of the nitrogen and carbon atoms in the molecule came to stand out.

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.

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

I have lived much of my life among molecules. They are good company. 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? I tell them, Try to feel like a molecule; and if you work hard, who knows? Some day you may get to feel like a big molecule!

Each one of us is a set of shifting molecules, spinning in ecstasy.