In describing a protein it is now common to distinguish the primary, secondary and tertiary structures. The primary structure is simply the order, or sequence, of the amino-acid residues along the polypeptide chains. This was first determined by Sanger using chemical techniques for the protein insulin, and has since been elucidated for a number of peptides and, in part, for one or two other small proteins. The secondary structure is the type of folding, coiling or puckering adopted by the polypeptide chain: the a-helix structure and the pleated sheet are examples. Secondary structure has been assigned in broad outline to a number of librous proteins such as silk, keratin and collagen; but we are ignorant of the nature of the secondary structure of any globular protein. True, there is suggestive evidence, though as yet no proof, that a-helices occur in globular proteins, to an extent which is difficult to gauge quantitatively in any particular case. The tertiary structure is the way in which the folded or coiled polypeptide chains are disposed to form the protein molecule as a three-dimensional object, in space. The chemical and physical properties of a protein cannot be fully interpreted until all three levels of structure are understood, for these properties depend on the spatial relationships between the amino-acids, and these in turn depend on the tertiary and secondary structures as much as on the primary. Only X-ray diffraction methods seem capable, even in principle, of unravelling the tertiary and secondary structures.
Co-author with G. Bodo, H. M. Dintzis, R. G. Parrish, H. Wyckoff, and D. C. Phillips

It is one of the striking generalizations of biochemistry—which surprisingly is hardly ever mentioned in the biochemical text-books—that the twenty amino acids and the four bases, are, with minor reservations, the same throughout Nature. As far as I am aware the presently accepted set of twenty amino acids was first drawn up by Watson and myself in the summer of 1953 in response to a letter of Gamow's.

It is, I believe, justifiable to make the generalization that anything an organic chemist can synthesize can be made without him. All he does is increase the probability that given reactions will 'go.' So it is quite reasonable to assume that given sufficient time and proper conditions, nucleotides, amino acids, proteins, and nucleic acids will arise by reactions that, though less probable, are as inevitable as those by which the organic chemist fulfills his predictions. So why not self-duplicating virus-like systems capable of further evolution?

Our conception of a native protein molecule (showing specific properties) is the following. The molecule consists of one polypeptide chain which continues without interruption throughout the molecule (or, in certain cases, of two or more such chains); this chain is folded into a uniquely defined configuration, in which it is held by hydrogen bonds between the peptide nitrogen and oxygen atoms and also between the free amino and carboxyl groups of the diamino and dicarboxyl amino acid residues.
The characteristic specific properties of native proteins we attribute to their uniquely defined configurations.
The denatured protein molecule we consider to be characterized by the absence of a uniquely defined configuration.
[Co-author with American chemist, Linus Pauling (1901-94)]

The language of the genes has a simple alphabet, not with twenty-six letters, but just four. These are the four different DNA bases—adenine, guanine, cytosine and thymine (A, G, C and T for short). The bases are arranged in words of three letters such as CGA or TGG. Most of the words code for different amino acids, which themselves are joined together to make proteins, the building blocks of the body.