Polypeptide Quotes (2 quotes)
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
Co-author with G. Bodo, H. M. Dintzis, R. G. Parrish, H. Wyckoff, and D. C. Phillips
'A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-ray Analysis', Nature (1958) 181, 662.
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 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)]
'On the Structure of Native, Denatured, and Coagulated Proteins', Proceedings of the National Academy of Sciences of the United States of America (1936), 22, 442-3.
In science it often happens that scientists say, 'You know that's a really good argument; my position is mistaken,' and then they would actually change their minds and you never hear that old view from them again. They really do it. It doesn't happen as often as it should, because scientists are human and change is sometimes painful. But it happens every day. I cannot recall the last time something like that happened in politics or religion.
(1987) -- 
