Abstract
SINCE the geometrical problem of protein structure is mainly that of the configuration of the polypeptide chains, the geometry of the peptide link itself is a matter of prime importance. However, very few crystal-structure data have yet been published from which precise dimensions of the peptide link may be derived. We have recently carried out a three-dimensional X-ray analysis of the structure of glycyl-L-asparagine which provides an additional source of these data. Our analysis also provides information concerning the molecular configuration of asparagine, an amino-acid the structure of which has recently been discussed in Nature by Steward and Thompson1.
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References
Steward, F. C., and Thompson, J. F., Nature, 169, 738 (1952).
Beevers, C. A., and Robertsen, J. H., Acta Cryst., 3, 164 (1950).
Donohue, J., and Trueblood, K. N., Acta Cryst., 5, 414 (1952).
Pauling, L., and Corey, R. B., Proc. U.S. Nat. Acad. Sci., 37, 235 (1951).
Senti, F., and Harker, D., J. Amer. Chem. Soc., 62, 2008 (1940).
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KATZ, L., PASTERNAK, R. & COREY, R. Configuration of the Peptide Link and of Asparagine in Glycyl-L-Asparagine. Nature 170, 1066 (1952). https://doi.org/10.1038/1701066a0
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DOI: https://doi.org/10.1038/1701066a0
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