• 1 January 1982
    • journal article
    • research article
    • Vol. 20  (2) , 154-158
Abstract
1H spectra at 270 MHz of the .beta.h[human]-endorphin glycyl residues in aqueous solution are reported. The chemical shifts, coupling constants and temperature coefficients are compared with those of the glycyl residues in Met-enkephalin and in a random coil model peptide. The local conformation of Tyr-Gly-Gly-Phe-segment observed in Met-enkephalin is maintained in .beta.h-endorphin.

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