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

Author(s)

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

Affiliation

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

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

• Document type: Journal article
• Source: SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY; v. 123, p. 482-489, APR 5 2014.
• Web of Science Citations: 8

Abstract

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)

• FAPESP's process: 11/01170-1 - Physicochemical studies of organic compounds: long range inractions and conformational analysis of organofluorine compounds.
• Grantee: Rodrigo Antonio Cormanich
• Support Opportunities: Scholarships in Brazil - Doctorate
• FAPESP's process: 12/03933-5 - Conformational equilibria and intramolecular interactions for a series of amino-acids: theoretical and experimental approaches
• Grantee: Roberto Rittner Neto
• Support Opportunities: Regular Research Grants