Proton nuclear magnetic resonance parameters are reported for DMSO‐d6 solutions of the eosinophil chemotactic tetrapeptides, Val1‐Gly2‐Ser3‐Glu4and Ala1‐Gly2‐Ser3‐Glu4, as well as three analogues of the Val1tetrapeptide, d‐Val1, Ala2and Ala3. The synthesis of Val‐(S)‐[α‐2H1] Gly‐Ala‐Glu, in which the glycine has been stereospecifically deuterated in the Hα3position, has allowed the assignment of the 1H resonances belonging to individual Hα2and Hα3glycine methylene protons. Simulation of the glycine ABX spin system yields two vicinal coupling constants which are consistent with a highly preferred conformation about the glycine HN‐Cαbond. The chemical shifts, coupling constants, temperature coefficients of amide proton chemical shifts and calculated side chain rotamer populations are reported for all peptides, The coupling constant analysis and temperature coefficients of amide proton chemical shifts together suggest that a type I β‐turn conformation is preferred by the Ala3analogue. The 1H n.m.r. parameters of the other peptides suggest that these can also adopt a β‐turn conformation in DMSO. There are. however, considerable differences in the extent of conformational averaging undergone by the various peptides. © 1985 Munksgaard International Publishers Ltd.