Fast Forward Maximum entropy reconstruction of sparsely sampled data. 2012

Nicholas M Balsgart, and Thomas Vosegaard
Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry, Aarhus University, DK-8000 Aarhus C, Denmark.

We present an analytical algorithm using fast Fourier transformations (FTs) for deriving the gradient needed as part of the iterative reconstruction of sparsely sampled datasets using the forward maximum entropy reconstruction (FM) procedure by Hyberts and Wagner [J. Am. Chem. Soc. 129 (2007) 5108]. The major drawback of the original algorithm is that it required one FT and one evaluation of the entropy per missing datapoint to establish the gradient. In the present study, we demonstrate that the entire gradient may be obtained using only two FT's and one evaluation of the entropy derivative, thus achieving impressive time savings compared to the original procedure. An example: A 2D dataset with sparse sampling of the indirect dimension, with sampling of only 75 out of 512 complex points (15% sampling) would lack (512-75)×2=874 points per ν(2) slice. The original FM algorithm would require 874 FT's and entropy function evaluations to setup the gradient, while the present algorithm is ∼450 times faster in this case, since it requires only two FT's. This allows reduction of the computational time from several hours to less than a minute. Even more impressive time savings may be achieved with 2D reconstructions of 3D datasets, where the original algorithm required days of CPU time on high-performance computing clusters only require few minutes of calculation on regular laptop computers with the new algorithm.

UI MeSH Term Description Entries
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D000465 Algorithms A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task. Algorithm
D001330 Electronic Data Processing Applications that store and process large quantities of data. Automatic Data Processing,Bar Codes,Computer Data Processing,Data Processing, Automatic,Information Processing, Automatic,Optical Readers,Information Processing,Automatic Information Processing,Bar Code,Codes, Bar,Data Processing, Computer,Data Processing, Electronic,Optical Reader,Processing, Automatic Data,Processing, Automatic Information,Processing, Computer Data,Processing, Electronic Data,Processing, Information
D019277 Entropy The measure of that part of the heat or energy of a system which is not available to perform work. Entropy increases in all natural (spontaneous and irreversible) processes. (From Dorland, 28th ed) Entropies

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