Isotope-edited FTIR in H2O: determination of the conformation of specific residues in a model α-helix peptide by 13C labeled carbonyls

Shanghao Li; Sneha Potana; Donnan J. Keith; Chengshan Wang; Roger M. Leblanc

doi:10.1039/C4CC00991F

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Isotope-edited FTIR in H₂O: determination of the conformation of specific residues in a model α-helix peptide by ¹³C labeled carbonyls†

Shanghao Li,‡^a Sneha Potana,‡^b Donnan J. Keith,^b Chengshan Wang*^b and Roger M. Leblanc*^a

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* Corresponding authors

^a Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Fl 33146, USA
E-mail: rml@miami.edu
Fax: +1 305-284-4571
Tel: +1 305-284-2194

^b Department of Chemistry, Middle Tennessee State University, 1301 East Main Street, Murfreesboro, TN 37132, USA
E-mail: chengshan.wang@mtsu.edu
Fax: +1 615-494-7963

Abstract

Isotope-edited FTIR spectroscopy has been shown to be able to determine peptide's structure in the residue level in D₂O, which is not a physiological solvent. Here, attenuated total reflection technique was utilized to successfully apply isotope-edited FTIR spectroscopy in H₂O to determine the conformation of specific residues in a model peptide.

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Article information

DOI: https://doi.org/10.1039/C4CC00991F
Article type: Communication
Submitted: 06 Feb 2014
Accepted: 22 Feb 2014
First published: 24 Feb 2014

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Chem. Commun., 2014,50, 3931-3933

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Isotope-edited FTIR in H₂O: determination of the conformation of specific residues in a model α-helix peptide by ¹³C labeled carbonyls

S. Li, S. Potana, D. J. Keith, C. Wang and R. M. Leblanc, Chem. Commun., 2014, 50, 3931 DOI: 10.1039/C4CC00991F

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