Abstract
Two crystal structures of a nonapeptide (anhydrous and hydrated) containing the amino acid residue alpha, alpha-di-n-butylglycyl, reveal a mixed 3(10)-/alpha-helical conformation. Residues 1-7 adopt phi, psi values in the helical region, with Val(8) being appreciably distorted. The Dbg residue has phi, psi values of -40, -37 degrees and -46, -40 degrees in the two crystals with the two butyl side chains mostly extended in each. Peptide molecules in the crystals pack into helical columns. The crystal parameters are: C50H91N9O12, space group P2(1), with a = 9.789(1) A, b = 20.240(2) A, c = 15.998(3) A, beta = 103.27(1); Z = 2, R = 10.3% for 1945 data observed > 3 sigma (F) and C50H91N9O12.3H2O, space group P2(1), with a = 9.747(3) A, b = 21.002(8) A, c = 15.885(6) A, beta = 102.22(3) degrees, Z = 2, R = 13.6% for 2535 data observed > 3 sigma (F). The observation of a helical conformation at Dbg suggests that the higher homologs in the alpha, alpha-dialkylated glycine series also have a tendency to stabilize peptide helices.
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