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Can I read Effect of the side group on the helix-forming tendency of α-alkyl-β-L-aspartamyl residues on EtoBox?
Effect of the side group on the helix-forming tendency of α-alkyl-β-L-aspartamyl residues by Carlos Alemán; Juan J. Navas; Sebastián Muñoz-Guerra is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Effect of the side group on the helix-forming tendency of α-alkyl-β-L-aspartamyl residues about?
The conformational preferences of the monomeric units of a series of poly(a-alkylb-L-aspartate)s were examined by quantum mechanical calculations. a-Alkyl-b-aspartamyl moligopeptides with a number of residues m ranging from 1 to 7 and arranged in the conformations experimentally observed for their corresponding polymers were computed. Both their total relative energies and their cooperative energy differences were compared as a function of the length of the oligopeptide and the nature of the alkyl side group. Results revealed that the 13/4 helical arrangement is the most stable structure for the isolated polymer chain for any side group, although a 17/4 helix becomes favored in the case of methyl and ethyl groups due to the packing effects. On the other hand, the stability of the 4/1 helix appears to be the preferred conformation for side groups with a branched constitution.
Who reads Effect of the side group on the helix-forming tendency of α-alkyl-β-L-aspartamyl residues?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Carlos Alemán; Juan J. Navas; Sebastián Muñoz-Guerra
- Publisher
- Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)
- Published
- 1997
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)
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