A helical peptide containing a majority of valyl residues. Crystal structure of t-butyloxycarbonyl-(L-valyl-α-aminoisobutyryl) 3 -L-valyl methyl ester monohydrate
作者： A.K. FRANCIS , E.K.S. VIJAYAKUMAR , P. BALARAM , M. VIJAYAN
DOI: 10.1111/J.1399-3011.1985.TB03199.X
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摘要: The monohydrate of the heptapeptide t-butyloxycarbonyl-(L-valyl-α-aminoiso-butyryl)3-L-valyl methyl ester crystallizes in orthorhombic space group P212121 with four molecules a unit cell dimensions α= 9.375, b = 19.413 and c 25.878 AA. structure has been solved by direct methods refined to an R value 0.059 for 3633 observed reflections. molecule exists as slightly distorted 310-helix stabilized five 4 -> 1 intramolecular hydrogen bonds, indicating overwhelming influence α-aminoisobutyryl (Aib) residues dictating helical fold even when majority peptide have low intrinsic propensity be helices. Contrary what is expected structures, valyl side chains, two which are disordered, exhibit all three possible conformations. arrange themselves head-to-tail fashion along c-axis. columns thus generated pack nearly hexagonally crystal.
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