Literature DB >> 20121194

Poisson-gap sampling and forward maximum entropy reconstruction for enhancing the resolution and sensitivity of protein NMR data.

Sven G Hyberts1, Koh Takeuchi, Gerhard Wagner.   

Abstract

The Fourier transform has been the gold standard for transforming data from the time domain to the frequency domain in many spectroscopic methods, including NMR spectroscopy. While reliable, it has the drawback that it requires a grid of uniformely sampled data points, which is not efficient for decaying signals, and it also suffers from artifacts when dealing with nondecaying signals. Over several decades, many alternative sampling and transformation schemes have been proposed. Their common problem is that relative signal amplitudes are not well-preserved. Here we demonstrate the superior performance of a sine-weighted Poisson-gap distribution sparse-sampling scheme combined with forward maximum entropy (FM) reconstruction. While the relative signal amplitudes are well-preserved, we also find that the signal-to-noise ratio is enhanced up to 4-fold per unit of data acquisition time relative to traditional linear sampling.

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Year:  2010        PMID: 20121194      PMCID: PMC2825045          DOI: 10.1021/ja908004w

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


  7 in total

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Journal:  J Am Chem Soc       Date:  2007-03-28       Impact factor: 15.419

6.  FM reconstruction of non-uniformly sampled protein NMR data at higher dimensions and optimization by distillation.

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  7 in total
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