Protein Folding Quotes

Alzheimer's disease starts when a protein that should be folded up properly misfolds into a kind of demented origami.

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

There is no cure for prions. They are a protein-based disease that, among other things, targets and transforms your brain. The symptoms reveal themselves differently in each host, and you might go months or you might go years before you realize you're infected.

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

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.

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

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

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

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.

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.

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

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

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.

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.

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.

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.

Serum albumin is a well-defined protein, but no laboratory has yet attempted to ascertain its full chemical structure.

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.

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.