The free induction decay (FID) is a function representing the decay of transverse magnetization as a function of time after the application of a pulse (or pulse sequence). The NMR spectrum is obtained by Fourier transforming the FID. All of the information in the NMR spectrum (line width, intensity, phase, line shape ....) is contained in the FID. Knowledge of what part of the FID represents a particular property of an NMR spectrum allows a user to process the raw time domain data in a way that maximizes the quality and information content of the processed frequency domain spectrum. The figure below shows the real component of the complex FID for a sample in which there is a single resonance. The FID is labelled in terms of its information content.
The shape of the envelope of the overall decay defines the line shape of the NMR resonance. Exponential decays yield Lorentzian line shapes. The frequency in the FID represents the offset of the resonance from the carrier frequency or in other words, how far the resonance is from the center of the spectrum. The higher the frequency, the further off-resonance the peak. The FID for an on-resonance peak is a simple decaying exponential with no oscillation frequency present. The first point of the FID contains the integrated intensity and phase information. Since time and frequency are reciprocals of one another, the duration of the decay before it disappears into the noise determines the sharpness of the NMR resonances and ultimately the resolution in cases where there is more than one resonance in the spectrum. The longer the decay - the narrower the lines. The early portion of the FID (short time) defines the broad features (wide frequency distributions) whereas the the latter portion of the FID (long time) defines the sharp features (narrow frequency distributions). Also, since the FID is a decaying function, the early portion has a higher signal-to-noise ratio than the latter portion. With this knowledge its is very easy to understand how best to apply apodization functions to the raw data for the purpose line broadening and resolution enhancement. Processing techniques such as zero filling, forward linear prediction, backward linear prediction and signal-to-noise optimization as well as spectral artifacts such as truncation errors, baseline roll and receiver saturation errors are easily understood with knowledge of the information content in the FID.
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[NMR paper] Determination of the casein content in bovine milk by 31P-NMR.
Determination of the casein content in bovine milk by 31P-NMR.
Related Articles Determination of the casein content in bovine milk by 31P-NMR.
J Dairy Res. 2002 Aug;69(3):411-8
Authors: Belloque J, Ramos M
The relative proportion of caseins to total protein is a parameter that can be used to control the protein quality in standardised milk, an increasing tendency in dairy industries. 31P-NMR was used to analyse the casein content of milk, by the quantitation of the area under the resonances belonging to SerP, and using methylenediphosphonic...
[NMR paper] Quantitative evaluation of water content in a solid protein by deuterium NMR.
Quantitative evaluation of water content in a solid protein by deuterium NMR.
Related Articles Quantitative evaluation of water content in a solid protein by deuterium NMR.
Biochim Biophys Acta. 1992 Feb 26;1119(2):178-84
Authors: Tamura A, Akasaka K
A method for evaluating absolute water content in a solid protein based on deuterium NMR measurements in solution is described. By dissolving the hydrated solid protein, which has been specifically deuterium-labeled, into deuterium-depleted water and by comparing the deuterium NMR signal intensity...
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[NMR paper] Exploring the dynamic information content of a protein NMR structure: comparison of a
Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
Proteins. 1999 Jul 1;36(1):87-110
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