14 March 1960

The Nobel Committee for Chemistry

Stockholm 50, SWEDEN

Gentlemen:

I write at the present time to inform you that I propose to nominate Professor Robert Brainard Corey for the Nobel Prize in Chemistry for 1961.

Professor Corey was born in Springfield, Massachusetts, on 19 August 1897. He has been a member of the staff of the California Institute of Technology from 1937 to the present time.

Since 1937 Professor Corey has worked steadily and effectively on a program of determination of the structure of proteins and related substances by the x-ray diffraction method. Other investigators have also been attacking this problem. It is to Corey, however, that we owe the major credit for having made possible the significant progress that has occurred. He made this progress possible through his successful program of determination of the structure of amino acids, simple peptides, and other simple substances closely related to proteins. Through this program of research he and he alone, with the assistance of his collaborators in the California Institute of Technology, obtained the basic structural information about the detailed molecular dimensions of peptides that has been the basis of all the progress in protein structure. I shall accordingly propose, when nominations are due for the Nobel Prize for Chemistry in 1961, that Professor Corey be awarded this Prize for his determination by the method of x-ray diffraction of the precise molecular structure of amino acids and peptides and the polypeptide chain, which has led to the elucidation of the detailed molecular structure of proteins.

In 1937, when Corey began his series of investigations, there had not been determined the precise structure of any amino acid or any simple peptide or any other simple substance closely related to the polypeptide chains of proteins, and there was much doubt not only about the structures of polypeptide chains of proteins, but also of simple peptides and amino acids. The first structure of this sort determined by Corey was that of diketopiperazine, in 1938. In collaboration with students and assistants, he then made precise structure determinations of glycine, alanine, and many other amino acids and related substances. For about ten years the structures determined by him and his collaborators were the only ones available to provide information relating to the structure of proteins.

Corey discovered that the substances related to polypeptide chains showed striking constancy of interatomic distances, bond angles and other structural features including, especially planarity of the amide group and formation of hydrogen-bonds between the hydrogen atom attached to nitrogen in this group and the carbonyl oxygen atom, with hydrogen-bond length always close to 2.8 A. These results allowed Corey to make detailed predictions about stable configurations of polypeptide chains in proteins. These detailed predictions then led to the formulation of certain important ways of coiling polypeptide chains, especially the alpha helix and the pleated sheets. Corey and his collaborators were able to present evidence for the occurance off the alpha helix in some fibrous proteins and of pleated sheets in other fibrous proteins. In particular, they were able to carry out a nearly complete structure determination of Bombyx mori silk and of Tussah silk fibroin.

Evidence has been presented by a number of investigations that the alpha helix is also an important structural feature of globular proteins. In particular, in the last year J.C. Kendrew and his collaborators of Cambridge University have obtained strong evidence for the existence of segments of polypeptide chains with the alpha-helix structure in molecules of myoglobin, and the results obtained by M. Perutz and his collaborators in Cambridge University for hemoglobin support the assignment of a similar structure to that protein. It is clear that the conclusion reached by Kendrew about the alpha helix in myoglobin could probably have not been reached if Corey had not carried out his fundamental investigations of precise dimensions of the polypeptide chain.

It has been my opinion that up to very recently the evidence for the existence of the alpha helix in globular proteins has not been conclusive, but that the work of Kendrew, published in Nature in February 1960, is essentially incontrovertible in showing that segments of the alpha helix with the right-handed twist are present in this globular protein. It is largely because the studies of globular proteins have been inconclusive until recently that I have delayed recommending Professor Corey for the Nobel Prize for Chemistry until now, and it is because of the delay in publication of Dr. Kendrew's results on myoglobin until February 1960 that my nomination of Corey for the Nobel Prize for Chemistry has to be postponed until February 1961.

It is my opinion that the researches by Robert B. Corey on the detailed molecular structure of amino acids and peptides and of the polypeptide chain are of such great and fundamental significance as to justify the award to him of the Nobel Prize in Chemistry, and it is for this reason that I propose to nominate him for the Prize in 1961.

Professor Sir Lawrence Bragg has communicated to me his nomination of M. F. Perutz and J. C. Kendrew for the Nobel Prize in Physics for 1960, and also of Dorothy Crowfoot Hodgkin. He has proposed Perutz and Kendrew for the Prize for their work on the detailed molecular structure of the globular proteins, especially hemoglobin and myoglobin, which has revealed that a significant part of the polypeptide chains in the molecules have the configuration of the alpha helix.

It is my opinion that the work of Kendrew and of Perutz might well justify the award of the Nobel Prize or a part of a Nobel Prize to them. I feel strongly, however, that no Nobel Prize should be awarded for the investigation of the detailed molecular structure of proteins without the inclusion of Robert Brainard Corey, and that if a Nobel Prize were to be awarded in this field, it should be to Robert Brainard Corey, for his pioneering work in determining the precise molecular structure of polypeptide chains and his participation in the determination of the most important configurations of polypeptide chains in proteins, and not to Perutz and Kendrew. A possibility that seems to me to be a reasonable one is that the Nobel Prize for Chemistry for 1961 be divided, with one half being given to Corey for his contributions to this field and the other half to Kendrew and Perutz.

Sincerely Yours,

Linus Pauling:jh

cc: The Nobel Comm. for Chemistry, Prof. Sir Lawrence Bragg