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|Title:||Phenylalanine and tyrosine methyl ester intramolecular interactions and conformational analysis by 1H NMR and infrared spectroscopies and theoretical calculations|
|Author:||Cormanich, Rodrigo A.|
Ducati, Lucas C.
Tormena, Cláudio F.
|Abstract:||Amino acid conformational analysis in solution are scarce, since these compounds present a bipolar zwitterionic structure ((+)H3NCHRCOO(-)) in these media. Also, intramolecular hydrogen bonds have been classified as the sole interactions governing amino acid conformational behavior in the literature. In the present work we propose phenylalanine and tyrosine methyl ester conformational studies in different solvents by (1)H NMR and infrared spectroscopies and theoretical calculations. Both experimental and theoretical results are in agreement and suggest that the conformational behavior of the phenylalanine and tyrosine methyl esters are similar and are dictated by the interplay between steric and hyperconjugative interactions.|
Amino acid conformational analysis in solution are scarce, since these compounds present a bipolar zwitterionic structure (+H3NCHRCOO−) in these media. Also, intramolecular hydrogen bonds have been classified as the sole interactions governing amino acid
Espectroscopia de infravermelho
Ligação de hidrogênio
|Citation:||Spectrochimica Acta. Part A, Molecular And Biomolecular Spectroscopy. v. 123, p. 482-9, 2014-Apr.|
|Appears in Collections:||IQ - Artigos e Outros Documentos|
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