ISSN:
1573-8388
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Summary 1. A conformational analysis of N-acetyl-L-leucine methylamide has been performed. The interdependence of the conformational states of the main and side chains of the molecule has been investigated. The most suitable orientation of the side chain corresponds to the values of the anglesx 1=x 2=180° and −60°. The overall minimum is located in the B region. 2. The validity of the assignment of leucine to the alanine stereochemical series has been shown. 3. To evaluate the contribution to the stability of the optimum conformations for the entropy of the side chain, conformational maps have been obtained of the statistical sums with a variation at each point of the angles ϕ and ψ of rotation around the Cα-Cγ and Cβ-Cγ bonds from 0 to −160°. 4. The optimum forms of N-acetyl-L-leucine methylamide have been compared with the conformations of leucine residues in proteins. A satisfactory agreement has been obtained between the theoretical and experimental values.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00570671
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