Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/201095
Type: Artigo de periódico
Title: Phenylalanine And Tyrosine Methyl Ester Intramolecular Interactions And Conformational Analysis By (1)h Nmr And Infrared Spectroscopies And Theoretical Calculations.
Author: Cormanich, Rodrigo A
Ducati, Lucas C
Tormena, Cláudio F
Rittner, Roberto
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.
Subject: Hydrogen Bonding
Magnetic Resonance Spectroscopy
Molecular Conformation
Phenylalanine
Spectrophotometry, Infrared
Tyrosine
(1)h Nmr Spectroscopy
Amino Acid Methyl Ester Derivatives
Conformational Analysis
Infrared Spectroscopy
Intramolecular Hydrogen Bonding
Stereoelectronic Effects
Rights: fechado
Identifier DOI: 10.1016/j.saa.2013.12.088
Address: http://www.ncbi.nlm.nih.gov/pubmed/24434201
Date Issue: 2014
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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