Results 1 to 10 of about 340,947 (357)
NMR Spectroscopy in Bioinorganic Chemistry
CHIMIA, 2012 Multinuclear and multidimensional nuclear magnetic resonance (NMR) spectroscopy is applied in our groups to gain insights into the role of metal ions for the function and structure of large biomolecules. Specifically, NMR is used i) to investigate how metal ions bind to nucleic acids and thereby control the folding and structure of RNAs, ii ...
Donghi, Daniela +3 more
openaire +7 more sources
Hyperdimensional NMR Spectroscopy [PDF]
Journal of the American Chemical Society, 2006 Hyperdimensional NMR describes the multiple interactions between a large number, N, of coupled nuclear spins. We show how to construct a hypothetical N-dimensional spectrum from a limited set of low-dimensional measurements, exploiting the concept of projection-reconstruction.
Eriks, Kupce, Ray, Freeman
openaire +2 more sources
In-Cell NMR Spectroscopy [PDF]
ChemBioChem, 2005 The role of a protein inside a cell is determined by both its location and its conformational state. Although fluorescence techniques are widely used to determine the cellular localization of proteins in vivo, these approaches cannot provide detailed information about a protein's three-dimensional state.
Zach, Serber +3 more
openaire +4 more sources
In-cell NMR spectroscopy [PDF]
Progress in Nuclear Magnetic Resonance Spectroscopy, 2011 Interactions between biological macromolecules give rise to and regulate biological activity. This activity is manifest through structural dynamics and changes in the macromolecular structures that comprise these interactions [1-3]. Until recently, mostly in vitro techniques have been used to study macromolecular interactions that govern biological ...
Andres Y, Maldonado +2 more
openaire +2 more sources
Diffusion NMR spectroscopy [PDF]
NMR in Biomedicine, 2001 AbstractMR offers unique tools for measuring molecular diffusion. This review focuses on the use of diffusion‐weighted MR spectroscopy (DW‐MRS) to non‐invasively quantitate the translational displacement of endogenous metabolites in intact mammalian tissues.
Nicolay, K. +4 more
openaire +2 more sources
Protein NMR spectroscopy [PDF]
Current Biology, 1998 Protein NMR spectroscopy does have its limitations. It has so far been used mainly for small proteins with molecular weight of less than 30 kDa, although a handful of publications have now reported the NMR study of proteins up to 40–50 kDa. Larger proteins typically have faster relaxation rates, which results in fatter NMR peaks that tend to merge with
openaire +2 more sources
NMR spectroscopy of nystose [PDF]
Carbohydrate Research, 1993 Sucrose (11, 1-kestose (21, and nystose (3) are the smallest inulin-related oligosaccharides1T2, which consist of (2 -+ l)-linked /3-D-fructofuranosyl residues, terminated by an a-D-glucopyranosyl unit in a (1 + 2) linkage. Several ‘H and 13C NMR assignments and some J,,, and J,,, values for inulin and inulin-related oligosaccharides have been ...
Vliegenthart, J.F.G. +4 more
openaire +3 more sources
Ultrahigh‐Resolution NMR Spectroscopy [PDF]
Angewandte Chemie International Edition, 2014 All psyched up: A flexible and general pure shift experiment (PSYCHE) has been developed that offers superior sensitivity, spectral purity, and tolerance of strong coupling over existing methods for broadband homonuclear decoupling. The partial spectra of estradiol in [D6]DMSO obtained by normal 1H NMR spectroscopy and PSYCHE are shown for comparison.
Foroozandeh, Mohammadali +5 more
openaire +4 more sources
NMR Spectroscopy for Metabolomics Research [PDF]
Metabolites, 2019 Over the past two decades, nuclear magnetic resonance (NMR) has emerged as one of the three principal analytical techniques used in metabolomics (the other two being gas chromatography coupled to mass spectrometry (GC-MS) and liquid chromatography coupled with single-stage mass spectrometry (LC-MS)). The relative ease of sample preparation, the ability
Abdul-Hamid Emwas +10 more
openaire +5 more sources
Single-crystal NMR spectroscopy
Progress in Nuclear Magnetic Resonance Spectroscopy, 2021 Single-crystal (SC) NMR spectroscopy is a solid-state NMR method that has been used since the early days of NMR to study the magnitude and orientation of tensorial nuclear spin interactions in solids. This review first presents the field of SC NMR instrumentation, then provides a survey of software for analysis of SC NMR data, and finally it highlights
openaire +4 more sources