Paul D. Boyer Quotes

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

Genes are effectively one-dimensional. If you write down the sequence of A, C, G and T, that's kind of what you need to know about that gene. But proteins are three-dimensional. They have to be because we are three-dimensional, and we're made of those proteins. Otherwise we'd all sort of be linear, unimaginably weird creatures.

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.

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

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.

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

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

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

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.

If we introduce iron complexly into ooporphyrin, we obtain haemin.

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.

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

It's nice to be able to look at one protein, but life is driven by the interactions between proteins, so it's really essential to be able to see multiple proteins at a time to understand these interactions.

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.

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.

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

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

That the primary effect of gene mutation may be as simple as the substitution of a single amino acid by another and may lead to profound secondary changes in protein structure and properties has recently been strongly indicated by the work of Ingram on hemoglobin.

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.

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

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.

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.

Every living being is also a fossil. Within it, all the way down to the microscopic structure of its proteins, it bears the traces if not the stigmata of its ancestry.