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Structural versatility of peptides from Cα,αdialkylated glycines: Linear Ac3c homo-oligopeptides

✍ Scribed by E. Benedetti; B. Di Blasio; V. Pavone; C. Pedone; A. Santini; M. Crisma; G. Valle; C. Toniolo

Publisher
Wiley (John Wiley & Sons)
Year
1989
Tongue
English
Weight
401 KB
Volume
28
Category
Article
ISSN
0006-3525

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✦ Synopsis

The crystal-state molecular structures of five linear A0,c homo-oligopeptides to the tetramer were determined by x-ray diffraction. The oligomem are H-(Aw),-OMe, Fmoc-(Ac+),-OMe . MeOH, Ac-(Ac&,-OMe, pBrBz-(Aq&OMe. H20, and t-Boc-(Ac+),-OMe . 2Hz0. The results indicate the propensity of the tri-and tetrapeptides to fold into type I &bends and distorted %,-helices, rqectively, in partial contrast to Aib, AGC, and AQC homo-peptides of comparable main-chain length, where regular type 111 /3-bends and %,-helical structures were found. When the influence of the constraints produced by the intramolecular H bonds of the C,,-type is absent, other less common structural featurea may be observed. The average geometry of the cyclopropyl group of the A0,c residue is found to be asymmetric and the N-C"-C' bond angle significantly expanded from the regular tetrahedral value.

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Structural versatility of peptides from
Structural versatility of peptides from Cα,α-dialkylated glycines. II. An IR absorption and 1H-nmr study of homo-oligopeptides from Cα,α-diethylglycine
✍ C. Toniolo; G. M. Bonora; A. Bavoso; E. Benedetti; B. Di Blasio; V. Pavone; C. P 📂 Article 📅 1988 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 416 KB

The conformational preferences of the N-trifluoroacetylated homo-peptides of C", "-diethylglycine from monomer to pentamer in chloroform solution were determined by using ir absorption and 'H-nmr. Intramolecular hydrogen bonding was found to be the dominant factor for all NH groups. The likely absen