Protein Structure Quotes

For me, each day begins and ends with wanting to learn a little more about the secrets of spider silk.

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

This seems highly likely, especially as it has been shown that in several systems mutations affecting the same amino acid are extremely near together on the genetic map.

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

Until 1985, when my lab found the protein they are made of, aquaporins hadn't yet been identified. There had been a controversy in biology for more than 100 years about how water moved through cells.

A meringue is really nothing but a foam. And what is a foam after all, but a big collection of bubbles? And what's a bubble? It's basically a very flimsy little latticework of proteins draped with water. We add sugar to this structure, which strengthens it. But things can, and do, go wrong.

No human can design a good enzyme, yet we are surrounded by them after 3.5 billion years of work by evolution.

Enzymes are masters of chemistry. They evolved over billions of years to perform specific biological functions. They make complex materials with virtually no waste.

As can be seen even by this limited number of examples proteins carry out amazingly diverse functions.

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

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

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

The basic structure of proteins is quite simple: they are formed by hooking together in a chain discrete subunits called amino acids.

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

An amino acid residue (other than glycine) has no symmetry elements. The general operation of conversion of one residue of a single chain into a second residue equivalent to the first is accordingly a rotation about an axis accompanied by translation along the axis. Hence the only configurations for a chain compatible with our postulate of equivalence of the residues are helical configurations.

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.

Inside of a living cell there are thousands of proteins that enable it to make more of itself and make your malaria drug, for instance. We don't understand those. We don't understand how they work together.

This led to the discovery that long chain fatty acids would remarkably stabilize serum albumin to heat denaturation, and would even reverse the denaturation by heat or concentrated urea solutions.

The prize was really for the molecule. In 1962, Osamu Shimomura discovered a protein in a jellyfish that caused it to glow bright green. With colleagues, 30 years later, I was able to insert this G.F.P. gene into bacteria and make them turn green.

Back in 1962, when I had by accident become the supervisor of Roberto Celis in Argentina, it occurred to me that antibody diversity might arise from the joining by disulphide bridges of a variety of small polypeptides in combinatorial patterns.

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

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

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.