Papers in this group
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Ever since its initial development, solution NMR spectroscopy has been used as a tool to study conformational exchange. Although many systems are amenable to relaxation dispersion approaches, cases involving highly skewed populations in slow…
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(1)H Nuclear magnetic resonance (NMR) spectroscopy (400 MHz) was used in the context of food surveillance to develop a reliable analytical tool to differentiate brands of cola beverages and to quantify selected constituents of the soft drinks. The…
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ABSTRACT: BACKGROUND: Red yeast rice (i.e., rice fermented with Monascus spp.), as a food supplement, is claimed to be blood cholesterol-lowering. The red yeast rice constituent monacolin K, also known as lovastatin, is an inhibitor of the…
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A methodology that utilizes (1)H-NMR spectroscopy has been developed to simultaneously analyze toxic terpenes (thujone and camphor), major polyphenolic compounds, the total antioxidant capacity (ORAC) and the Folin-Ciocalteu (FC) index in foods and…
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NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by…
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Selective isotopic labeling provides an unparalleled window within which to study the structure and dynamics of RNAs by high resolution NMR spectroscopy. Unlike commonly used carbon sources, the asymmetry of (13)C-labeled pyruvate provides selective…
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Characterization of the structure and dynamics of nucleic acids by NMR benefits significantly from position specifically labeled nucleotides. Here an E. coli strain deficient in the transketolase gene (tktA) and grown on glucose that is labeled at…
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A Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for quantifying millisecond time-scale chemical exchange at side-chain (1)H positions in proteins. Such experiments are not possible in a fully protonated molecule because of…
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Allostery is a fundamental process by which distant sites within a protein system sense each other. Allosteric regulation is such an efficient mechanism that it is used to control protein activity in most biological processes, including signal…
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Chemical shifts reflect the structural environment of a certain nucleus and can be used to extract structural and dynamic information. Proper calibration is indispensable to extract such information from chemical shifts. Whereas a variety of…
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The transformation of second-rank Cartesian tensors under rotation plays a fundamental role in the theoretical description of nuclear magnetic resonance experiments, providing the framework for describing anisotropic phenomena such as single crystal…
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Molecular dynamics are essential for life, and nuclear magnetic resonance (NMR) spectroscopy has been used extensively to characterize these phenomena since the 1950s. For the past 15 years, the Carr-Purcell Meiboom-Gill relaxation dispersion (CPMG…
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The backbone dynamics of the C-terminal SH2 domain of phospholipase C gamma 1 have been investigated. Two forms of the domain were studied, one in complex with a high-affinity binding peptide derived from the platelet-derived growth factor receptor…
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TROSY, Transverse Relaxation Optimized Spectroscopy, was developed more than a decade ago. Since that time, the 15N-1H HSQC-TROSY experiment has become the standard “fingerprint” correlation spectrum for proteins of high molecular weight. In…
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Many recently discovered noncoding RNAs do not fold into a single native conformation but sample many different conformations along their free-energy landscape to carry out their biological function. Here we review solution-state NMR techniques that…
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The 400 MHz (1) H NMR analysis of alcoholic beverages using standard pulse programs lacks the necessary sensitivity to detect minor constituents such as methanol, acetaldehyde or ethyl acetate. This study investigates the application of a shaped…