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Conformational studies of peptide systems. NMR and IR spectra of N-acetyl-alanyl-phenylalanine and N-acetyl-phenylalanyl-alanine ethyl esters.

โœ Scribed by V.F. Bystrov; S.L. Portnova; T.A. Balashova; V.I. Tsetlin; V.T. Ivanov; P.V. Kostetzky; Yu.A. Ovchinnikov


Publisher
Elsevier Science
Year
1969
Tongue
French
Weight
230 KB
Volume
10
Category
Article
ISSN
0040-4039

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โœฆ Synopsis


In a prwioua efndy, the conformational states of alanyl-alsnlne dipepti-~8 in solution have been elucidated: The study was largely based on the uependent of the NH-CE vicinal proton couplw constant upon the dihedral angle 8 between the ENC snd JJCCH planes: 3JIvHCrr P A ooE?e -B ~0.~8 +C sin2& Values for this tlepcnclence calculated on a IL;-360/60 computer for values the coefficients varying within the following limits (1)r 8.9 L A 4 9.8 Hz,


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โœ Chalakkal I. Jose; Anagha A. Belhekar; Mangala S. Agashe ๐Ÿ“‚ Article ๐Ÿ“… 1987 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 591 KB

NH stretching bands of N-acetyl-(glycine, L-alanine, L-leucine)-W-methylamides in dilute chloroform solution have shown that these dipeptides are present as a mixture of intramolecularly hydrogen-bonded five-membered ring species and nonhydrogen bonded species. Integrated absorption intensity measur