Abstract
THE need for a cyclic structure for certain proteins (for example, serum globulins) has been emphasized in a series of papers by Wrinch1,2. However, the hexacyclic carbon–nitrogen ring structure which she proposes has not been generally accepted, due partly to steric objections. It is believed at present that two-dimensional protein structures are formed by hydrogen bonding between polypeptide chains. In the present communication a new oxygen cross-bonded structure is suggested. It is characterized by ionic dissociation, and a double bond, at the peptide linkage. The structure is: where N* is either N− or (HNH)+ depending on whether the dissociation: or occurs. The amino-acid residues (R groups) and the H ions of (HNH)+ groups lie perpendicularly to the plane of the structure.
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References
Wrinch, D., Proc. Roy. Soc., A, 160, 59 (1937).
Wrinch, D., Phil. Mag., 30, 64 (1940).
Fraenkel-Conrat, H., and Ramachandran, L. K., Adv. Protein Chem., 14, 183 (1959).
Lucas, F., Shaw, J. T. B., and Smith, S. G., Adv. Protein Chem., 13, 225 (1958).
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BROWNE, P. Possibility of Ionic Dissociation at the Peptide Linkage. Nature 189, 658 (1961). https://doi.org/10.1038/189658a0
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DOI: https://doi.org/10.1038/189658a0
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