Spectral analysis of 1H coupled 13C spectra of the amino acids

Adaptive spectral library of amino acid 13C isotopomers and positional fractional 13C enrichments

Mika Tiainen (Corresponding Author), Hannu Maaheimo, Matthias Niemitz, Pasi Soininen, Reino Laatikainen

Research output: Contribution to journalArticleScientificpeer-review

14 Citations (Scopus)

Abstract

The natural abundance 1H‐coupled 13C NMR spectra of all proteogenic amino acids were measured in D2O at pH* 1. The accurate 1H,13C spin‐spin coupling constants were analyzed using total‐line‐shape fitting. The obtained spectral parameters can be used to establish a spectral library of amino acid 13C isotopomers. The adaptive spectral library principle is introduced and discussed in this article. The simulated spectra can be applied to quantification of 13C isotopomer mixtures of amino acids and, thus, for exploring metabolic pathways. Also a protocol for amino acid 13C isotopomer metabolomic profiling in 13C labeled glucose feeding experiments is outlined. The approach is suggested to give invaluable information about positional fractional 13C enrichments, which are not easily available by any other method.
Original languageEnglish
Pages (from-to)125 - 137
Number of pages13
JournalMagnetic Resonance in Chemistry
Volume46
Issue number2
DOIs
Publication statusPublished - 2008
MoE publication typeA1 Journal article-refereed

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Spectrum analysis
Amino acids
Amino Acids
Glucose
Nuclear magnetic resonance
Experiments

Keywords

  • NMR
  • 1H
  • 13C
  • amino acids
  • isotopomer distribution
  • isotopomers
  • spectral analysis
  • positional fractional enrichment
  • metabolic flux analysis

Cite this

@article{3824008769b649c08c52703028b16e05,
title = "Spectral analysis of 1H coupled 13C spectra of the amino acids: Adaptive spectral library of amino acid 13C isotopomers and positional fractional 13C enrichments",
abstract = "The natural abundance 1H‐coupled 13C NMR spectra of all proteogenic amino acids were measured in D2O at pH* 1. The accurate 1H,13C spin‐spin coupling constants were analyzed using total‐line‐shape fitting. The obtained spectral parameters can be used to establish a spectral library of amino acid 13C isotopomers. The adaptive spectral library principle is introduced and discussed in this article. The simulated spectra can be applied to quantification of 13C isotopomer mixtures of amino acids and, thus, for exploring metabolic pathways. Also a protocol for amino acid 13C isotopomer metabolomic profiling in 13C labeled glucose feeding experiments is outlined. The approach is suggested to give invaluable information about positional fractional 13C enrichments, which are not easily available by any other method.",
keywords = "NMR, 1H, 13C, amino acids, isotopomer distribution, isotopomers, spectral analysis, positional fractional enrichment, metabolic flux analysis",
author = "Mika Tiainen and Hannu Maaheimo and Matthias Niemitz and Pasi Soininen and Reino Laatikainen",
year = "2008",
doi = "10.1002/mrc.2140",
language = "English",
volume = "46",
pages = "125 -- 137",
journal = "Magnetic Resonance in Chemistry",
issn = "0749-1581",
publisher = "Wiley",
number = "2",

}

Spectral analysis of 1H coupled 13C spectra of the amino acids : Adaptive spectral library of amino acid 13C isotopomers and positional fractional 13C enrichments . / Tiainen, Mika (Corresponding Author); Maaheimo, Hannu; Niemitz, Matthias; Soininen, Pasi; Laatikainen, Reino.

In: Magnetic Resonance in Chemistry, Vol. 46, No. 2, 2008, p. 125 - 137.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Spectral analysis of 1H coupled 13C spectra of the amino acids

T2 - Adaptive spectral library of amino acid 13C isotopomers and positional fractional 13C enrichments

AU - Tiainen, Mika

AU - Maaheimo, Hannu

AU - Niemitz, Matthias

AU - Soininen, Pasi

AU - Laatikainen, Reino

PY - 2008

Y1 - 2008

N2 - The natural abundance 1H‐coupled 13C NMR spectra of all proteogenic amino acids were measured in D2O at pH* 1. The accurate 1H,13C spin‐spin coupling constants were analyzed using total‐line‐shape fitting. The obtained spectral parameters can be used to establish a spectral library of amino acid 13C isotopomers. The adaptive spectral library principle is introduced and discussed in this article. The simulated spectra can be applied to quantification of 13C isotopomer mixtures of amino acids and, thus, for exploring metabolic pathways. Also a protocol for amino acid 13C isotopomer metabolomic profiling in 13C labeled glucose feeding experiments is outlined. The approach is suggested to give invaluable information about positional fractional 13C enrichments, which are not easily available by any other method.

AB - The natural abundance 1H‐coupled 13C NMR spectra of all proteogenic amino acids were measured in D2O at pH* 1. The accurate 1H,13C spin‐spin coupling constants were analyzed using total‐line‐shape fitting. The obtained spectral parameters can be used to establish a spectral library of amino acid 13C isotopomers. The adaptive spectral library principle is introduced and discussed in this article. The simulated spectra can be applied to quantification of 13C isotopomer mixtures of amino acids and, thus, for exploring metabolic pathways. Also a protocol for amino acid 13C isotopomer metabolomic profiling in 13C labeled glucose feeding experiments is outlined. The approach is suggested to give invaluable information about positional fractional 13C enrichments, which are not easily available by any other method.

KW - NMR

KW - 1H

KW - 13C

KW - amino acids

KW - isotopomer distribution

KW - isotopomers

KW - spectral analysis

KW - positional fractional enrichment

KW - metabolic flux analysis

U2 - 10.1002/mrc.2140

DO - 10.1002/mrc.2140

M3 - Article

VL - 46

SP - 125

EP - 137

JO - Magnetic Resonance in Chemistry

JF - Magnetic Resonance in Chemistry

SN - 0749-1581

IS - 2

ER -