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Effect of phenyl ring position in the Cα-methylated α-amino acid side chain on peptide preferred conformation

✍ Scribed by C. Toniolo; M. Crisma; F. Formaggio; A. Polese; M. Doi; T. Ishida; E. Mossel; Q. Broxterman; J. Kamphuis

Publisher: Wiley (John Wiley & Sons)
Year: 1996
Tongue: English
Weight: 308 KB
Volume: 40
Category: Article
ISSN: 0006-3525
DOI: 10.1002/(sici)1097-0282(1996)40:5<523::aid-bip10>3.0.co;2-i

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✦ Synopsis

The preferred conformations of C"-methyl phenylglycine, C"-methyl phenylalanine, and C"-methyl homophenylalanine residues, as determined in model peptides (including homopeptides) by Fourier transform ir absorption, 'H-nmr, CD, and x-ray diffraction techniques, are compared with the aim of investigating the effect of phenyl ring position in the C"methylated amino acid side chain. This study shows that ( a ) 0-turn and 310-helical structures are preferentially adopted by peptides rich in these C"-methylated, aromatic a-amino acids and ( b ) turn and helix handedness is critically biased by the position of side-chain branching.

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✍ Cristina Peggion; Fernando Formaggio; Marco Crisma; Claudio Toniolo; Bernard Kap 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 136 KB

The lipophilic, chiral, C h -methylated h-amino acid L-(h Me)Aoc (2-methyl-2-amino-octanoic acid) was prepared using a chemo-enzymatic approach. Two series of terminally protected model peptides, from dimer through to hexamer, containing L-(h Me)Aoc in combination with either Gly or Aib, were synthe