Related ArticlesThe equilibrium unfolding of MerP characterized by multivariate analysis of 2D NMR data.
J Magn Reson. 2005 Jan;172(1):24-30
Authors: Berglund A, Brorsson AC, Jonsson BH, Sethson I
A general problem when analysing NMR spectra that reflect variations in the environment of target molecules is that different resonances are affected to various extents. Often a few resonances that display the largest frequency changes are selected as probes to reflect the examined variation, especially in the case, where the NMR spectra contain numerous resonances. Such a selection is dependent on more or less intuitive judgements and relying on the observed spectral variation being primarily caused by changes in the NMR sample. Second, recording changes observed for a few (albeit significant) resonances is inevitably accompanied by not using all available information in the analysis. Likewise, the commonly used chemical shift mapping (CSM) [Biochemistry 39 (2000) 26, Biochemistry 39 (2000) 12595] constitutes a loss of information since the total variation in the data is not retained in the projection into this single variable. Here, we describe a method for subjecting 2D NMR time-domain data to multivariate analysis and illustrate it with an analysis of multiple NMR experiments recorded at various folding conditions for the protein MerP. The calculated principal components provide an unbiased model of variations in the NMR spectra and they can consequently be processed as NMR data, and all the changes as reflected in the principal components are thereby made available for visual inspection in one single NMR spectrum. This approach is much less laborious than consideration of large numbers of individual spectra, and it greatly increases the interpretative power of the analysis.
Metabolic characterization of Palatinate German white wines according to sensory attributes, varieties, and vintages using NMR spectroscopy and multivariate data analyses
Metabolic characterization of Palatinate German white wines according to sensory attributes, varieties, and vintages using NMR spectroscopy and multivariate data analyses
Abstract 1H NMR (nuclear magnetic resonance spectroscopy) has been used for metabolomic analysis of â??Rieslingâ?? and â??Mueller-Thurgauâ?? white wines from the German Palatinate region. Diverse two-dimensional NMR techniques have been applied for the identification of metabolites, including phenolics. It is shown that sensory analysis correlates with NMR-based metabolic profiles of wine. 1H NMR data in combination...
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[NMR paper] Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate reveal
Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering.
Related Articles Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering.
J Mol Biol. 2002 Sep 27;322(4):841-9
Authors: Fowler SB, Best RB, Toca Herrera JL, Rutherford TJ, Steward A, Paci E, Karplus M, Clarke J
The mechanical unfolding of an immunoglobulin domain from the...
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[NMR paper] NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein i
NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance.
Related Articles NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance.
Biochemistry. 1998 Jun 30;37(26):9316-22
Authors: Qian H, Sahlman L, Eriksson PO, Hambraeus C, Edlund U, Sethson I
Mercuric ions are toxic to living organisms because of their strong affinity for cysteine residues in proteins. Some bacteria have developed a resistance...
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[NMR paper] Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis
Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
Biochemistry. 1997 May 27;36(21):6326-35
Authors: Ubbink M, Bendall DS
The complexes of horse ferrous and ferric cytochrome c with Cd-substituted pea plastocyanin have been characterized by nuclear magnetic resonance, in order to determine the binding sites and to study...
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[NMR paper] Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis
Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
Biochemistry. 1997 May 27;36(21):6326-35
Authors: Ubbink M, Bendall DS
The complexes of horse ferrous and ferric cytochrome c with Cd-substituted pea plastocyanin have been characterized by nuclear magnetic resonance, in order to determine the binding sites and to study...
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08-22-2010 03:03 PM
[NMR paper] A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydro
A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydrogenase of Escherichia coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydrogenase of Escherichia coli.
Biochemistry. 1996 Dec 24;35(51):16502-9
Authors: Sun ZY, Pratt EA, Simplaceanu V, Ho C
Partially folded protein intermediates have been observed by 19F-NMR spectroscopy during the equilibrium unfolding of the...
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[NMR paper] 1H NMR studies of the mercuric ion binding protein MerP: sequential assignment, secon
1H NMR studies of the mercuric ion binding protein MerP: sequential assignment, secondary structure and global fold of oxidized MerP.
Related Articles 1H NMR studies of the mercuric ion binding protein MerP: sequential assignment, secondary structure and global fold of oxidized MerP.
J Biomol NMR. 1993 Nov;3(6):613-26
Authors: Eriksson PO, Sahlman L
The oxidized form of the mercuric ion binding protein MerP has been studied by two-dimensional NMR. MerP, which is a periplasmic water-soluble protein with 72 amino acids, is involved in the...
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[Nature network NMR forum] Multivariate analysis of NMR spectra (0 replies)
Multivariate analysis of NMR spectra (0 replies)
Hi,
I am currently debating the benefit of different multivariate analysis methods for analysing NMR spectra and wondered if anyone had any ideas?
I have implemented principal components analysis (PCA) and canonical variates analysis (CVA). I am now looking into partial least squares discriminate analysis (PLS-DA).
My data contains a continuum of disease scores which I have categorised as Low Moderate and High. I would like to create a prediction model of disease state. The CVA analysis is supervised, so takes these...
The equilibrium unfolding of MerP characterized by multivariate analysis of 2D NMR da
Linear Mode
