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Structural versatility of peptides from Cα, α-disubstituted glycines: Crystal-state conformational analysis of homopeptides from Cα-methyl, Cα-benzylglycine [(αMe)Phe]n

✍ Scribed by Giovanni Valle; Monica Pantano; Fernando Formaggio; Marco Crisma; Claudio Toniolo; Gilles Précigoux; Gerlind Sulzenbacher; Wilhelmus H. J. Boesten; Quirinus B. Broxterman; Hans E. Schoemaker; Johan Kamphuis


Publisher
Wiley (John Wiley & Sons)
Year
1993
Tongue
English
Weight
688 KB
Volume
33
Category
Article
ISSN
0006-3525

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The molecular structures of four protected isovaline-(Iva-)containing peptides to the pentamer level have been determined by x-ray diffraction. The peptides are t-Boc-Ala-( S ) -1va-Ala-OMe ( t-Boc : tert-butyloxycarbonyl; OMe : methoxy) and its ( R ) -1va diastereomer, and t-Boc-[ Ala-( R ) -Iva],-

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Conformational energy computations on a derivative and a homo-dipeptide of C"\*"-diethylglycine were performed. In both cases the Nand C-terminal groups are blocked as acetamido and methylamido moieties, respectively. It was found that the C"3"-diethylglycine residues are conformationally restricted

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## Abstract The conformational preference of C^α,α^‐diphenylglycinc (Døg) and C^α,α^‐dibenzylglycine (Dbz) residues was assessed in selected derivatives and small peptides by conformational energy computations, ir absorption, ^1^H‐nmr, and x‐ray diffraction. Conformational energy computations on th

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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