Structure and conformation of linear peptides
- 1 February 1986
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 27 (2) , 160-164
- https://doi.org/10.1111/j.1399-3011.1986.tb01806.x
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.Keywords
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