Dr. Christian Anfinsen published The Molecular Basis of Evolution in 1959. It was partly a basic primer on genetics and evolution for chemists, and partly a manifesto for the importance of chemistry to molecular biology, genetics, and evolutionary theory. The book was Anfinsen’s statement of belief and motivation, and through it he inspired many younger scientists.

You can download and read The Molecular Basis of Evolution at https://profiles.nlm.nih.gov/ps/access/KKBBLS.pdf
pdf (18,226,034 Bytes)

Take a peek inside the book.

This chromatography column from Pharmacia Fine Chemicals is one kind used in Anfinsen’s laboratory for affinity chromatography, a method that he began using in the 1960s to purify samples of the protein Staphylococcal nuclease, which enabled him to pinpoint the exact positions of the 149 individual amino acid units and their peptide bonds.

Other types of chromatography separate molecules based on size, differences in chemical or physical interactions, or strength of their ionic interactions. In affinity chromatography, a molecule called a “ligand” that binds to a specific receptor, is anchored to solid support. When a solution is passed over it, the ligand binds to the specific molecule that has an “affinity,” or natural bond, with it. After the other components of the solution are washed away, the now purified molecule is stripped from its support.

Chromatography Column Artifacts page

Staphylococcal nuclease was the focus of extensive experimental work under Dr. Christian Anfinsen from about 1963 to 1975. This molecular model was built as part of the educational program of Protein Chemistry evening seminars for Research Associates conducted throughout the 1960’s by Drs. Anfinsen and David Davies. It’s based on the x-ray crystallographic analysis done at the Massachusetts Institute of Technology under the direction of Professor Albert Cotton.

Learn more on the Staphylococcal Nuclease Model page.

This is a historical organization chart of the original Laboratory of Cellular Physiology and Metabolism that was started by Dr. Christian Anfinsen at what was then the National Heart Institute (now the National Heart, Lung, and Blood Institute, NHLBI), when he was recruited by NIH director Dr. James Shannon in 1950.

Learn more on the Employee Organization Chart page.

Dr. Christian Anfinsen went through a lot of Genuine Whatman Filter Paper, No. 1 during his career. There are different grades of filter paper; No. 1 was labelled, “For ordinary work, retaining medium sized particles. Qualitative or rough quantitative.” It’s used in paper chromatography, a method that Anfinsen performed in many of his experiments, in which chemical substances are separated based on how far they migrate on the specially prepared piece of filter paper.

Learn more on the W. & R. Balston Ltd. Genuine Whatman Filter Paper page.

Anfinsen was always trying the newest technology to advance his research. In 1963, Bruce Merrifield at Rockefeller Institute developed the technique of solid-phase protein synthesis. In this method, the peptide is bound to an insoluble support, usually a bead, and any unreacted reagents left at the end of any step in the process are removed by a simple washing. Anfinsen tried this technique, but abandoned it because it could not handle large proteins like Staphylococcal nuclease. He kept this equipment, though, in case it could be used in other experiments.

Read Anfinsen’s thorough history of his experiments, including a discussion of solid phase peptide synthesis, in “Principles that Govern the Folding of Protein Chains,” Science, 20 July 1973, Volume 181, Number 4096.

Learn more on the Solid Phase Peptide Synthesizer page.

This capillary viscometer was created by NIH glassblowers especially for Dr. Waldo Fisher. Fisher had won a year in Dr. Christian Anfinsen’s laboratory (1971-72) through a U.S. Public Health Service Career Development Award. During that year, Fisher worked on the enzyme cytochrome c, using it as another example of Anfinsen’s Thermodynamic Hypothesis on the relation between a protein’s amino acid structure and its three-dimensional shape. Devices such as viscometers, which measure a liquid’s viscosity (thickness), were common in the 1960-70s, and were used in the physical characterization of proteins. This one was specially made to measure very small amounts of liquid.

Learn more on the NIH Glassblowers Capillary Viscometer artifact page.