| Autor: |
Toniolo C; C.N.R., Department of Organic Chemistry, University of Padova, Italy., Crisma M, Bonora GM, Klajc B, Lelj F, Grimaldi P, Rosa A, Polinelli S, Boesten WH, Meijer EM, et. al. |
| Jazyk: |
angličtina |
| Zdroj: |
International journal of peptide and protein research [Int J Pept Protein Res] 1991 Sep; Vol. 38 (3), pp. 242-52. |
| DOI: |
10.1111/j.1399-3011.1991.tb01435.x |
| Abstrakt: |
Conformational energy computations on Ac-L-(alpha Me)Val-NHMe indicate that turns and right-handed helical structures are particularly stable conformations for this chiral C alpha-methyl, C alpha-alkylglycyl residue. We have synthesized and characterized a variety of L-(alpha Me)Val derivatives and peptides (to the pentamer level). The results of the solution conformational analysis, performed using infrared absorption, 1H nuclear magnetic resonance, and circular dichroism, are in general agreement with those obtained from the theoretical investigation, in the sense that the L-(alpha Me)Val residue turns out to be a strong beta-turn and right-handed helix former. A comparison is also made with the conclusions extracted from published work on peptides rich in other C alpha-methyl, C alpha-alkylglycyl residues. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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