Structure and conformation of linear peptides

Abstract
The dipeptide, (DL)-alanyl-(DL)-norvaline, crystallizes in the monoclonic space group P21/c, with a=12.559(2)A, b=5.265(1), c=16.003(3), .beta.=103.53(2).degree., Z=4. The structure was solved by direct methods and refined to an R-value of 0.054 for 871 reflections with I > 2 .sigma.. The molecule exists as a zwitterion in the crystal. The peptide unit is trans and shows significant deviations from planarity (.DELTA..omega.=12.4.degree.). The peptide backbone adopts an extended conformation. The unit cell contains D-Ala-L-norval and its enantiomer. The molecular conformation and packing features show a striking resemblance to those for D-Ala-L-Met (1), and leads to the speculation that norvaline might act as an analog of methionine.

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