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AMINO ACID ANALYSIS AND THE STRUCTURE OF PROTEINS

Nature volume 150, page 127 (25 July 1942) | Download Citation

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Abstract

IN recent years X-ray crystallographers have made remarkable advances in the interpretation of protein structure, and it is becoming more and more evident that a stage has been reached when their views need to be reconciled with data obtained from accurate amino-acid analysis of the proteins concerned. In 1934 Astbury suggested that in gelatin the residues of glycine and hydroxyproline must repeat at regular intervals along the peptide chain, an idea developed in the following year by Bergmann and Niemann into a general hypothesis that (briefly) the 'frequency' of recurrence of any particular residue must be factorizable entirely by 2 and/or 3, as must also the total number of residues in the molecule, Evidence in its favour was adduced from analytical data for several proteins, including egg-albumin. The hypothesis has been criticized on various grounds, chief among them being that existing methods of analysis are in most cases not sufficiently quantitative to warrant the results being interpreted with the precision needed. What are believed to be quantitative estimations for the bases and dicarboxylic acids in edestin, egg-albumin and p-lactoglobulin have now been obtained.

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https://doi.org/10.1038/150127a0

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