A. Aubry et al., CRYSTAL-STRUCTURE ANALYSIS OF A BETA-TURN MIMIC IN HYDRAZINO PEPTIDES, International journal of peptide & protein research, 43(3), 1994, pp. 305-311
The crystal structures of four hydrazino peptides (Piv-Pro-h(N-alpha-B
zl)Gly-NHiPr 1, Piv-Pro-hAla-NHiPr 2, Mcc-hPro-NHiPr 3, and Boc-hPro-G
ly-N(OH)Me 4) deriving from the hydrazino analogues of glycine (hGly),
L-alanine (hAla) or L-proline (hPro) have been solved. They reveal a
common folded structure of the alpha-hydrazino acid residue characteri
zed by a bifurcated hydrogen bond closing an eight-membered cycle. Thi
s folded structure is topologically similar to the beta II'-turn in pe
ptides, and the CO-NH-N hydrazide link can be considered as a good tur
n-inducer in peptide analogues. (C) Munksgaard 1994.