Phenylalanine and tyrosine methyl ester intramolecular interactions and conformational analysis by H-1 NMR and infrared spectroscopies and theoretical calculations

Autor(es)

Cormanich, Rodrigo A. ^[1] ; Ducati, Lucas C. ^[2] ; Tormena, Claudio F. ^[1] ; Rittner, Roberto ^[1]

Afiliação do(s) autor(es)

^[1] Univ Estadual Campinas, Inst Chem, BR-13083970 Campinas, SP - Brazil

^[2] Univ Sao Paulo, Inst Chem, BR-05508900 Sao Paulo - Brazil

• Tipo de documento: Artigo Científico
• Fonte: SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY; v. 123, p. 482-489, APR 5 2014.
• Citações Web of Science: 8

Resumo

Amino acid conformational analysis in solution are scarce, since these compounds present a bipolar zwitterionic structure (+H3N-CHR-COO-) 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 H-1 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. (C) 2014 Elsevier B.V. All rights reserved. (AU)

• Processo FAPESP: 11/01170-1 - Estudos físico-químicos de compostos orgânicos: interações de longa distância e análise conformacional de compostos organofluorados
• Beneficiário: Rodrigo Antonio Cormanich
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 12/03933-5 - Equilíbrios conformacionais e interações intramoleculares em uma série de aminoácidos: abordagem teórica e experimental
• Beneficiário: Roberto Rittner Neto
• Modalidade de apoio: Auxílio à Pesquisa - Regular