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Nuclear Magnetic Resonance of Hyperpolarized Fluorine for Characterization of Protein–Ligand Interactions - American Chemical Society
Apr 28, 2023 - 3:59 PM - by nmrlearner
nmrlearner's Avatar Nuclear Magnetic Resonance of Hyperpolarized Fluorine for Characterization of Protein–Ligand Interactions American Chemical Society
Nuclear Magnetic Resonance of Hyperpolarized Fluorine for Characterization of Protein–Ligand Interactions - American Chemical Society
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0 Replies | 201 Views
[NMR paper] Urinary 1H NMR Metabolomic Analysis of Prenatal Maternal Stress Due to a Natural Disaster Reveals Metabolic Risk Factors for Non-Communicable Diseases: The QF2011 Queensland Flood Study
Apr 28, 2023 - 3:59 PM - by nmrlearner
nmrlearner's Avatar Urinary 1H NMR Metabolomic Analysis of Prenatal Maternal Stress Due to a Natural Disaster Reveals Metabolic Risk Factors for Non-Communicable Diseases: The QF2011 Queensland Flood Study

Prenatal stress alters fetal programming, potentially predisposing the ensuing offspring to long-term adverse health outcomes. To gain insight into environmental influences on fetal development, this QF2011 study evaluated the urinary metabolomes of 4-year-old children (n = 89) who were exposed to the 2011 Queensland flood in utero. Proton nuclear magnetic resonance spectroscopy was used to analyze urinary metabolic fingerprints based on maternal levels of objective hardship and subjective...

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0 Replies | 234 Views
[NMR paper] Interaction of Hyaluronan Acid with Some Proteins in Aqueous Solution as Studied by NMR
Apr 28, 2023 - 12:13 AM - by nmrlearner
nmrlearner's Avatar Interaction of Hyaluronan Acid with Some Proteins in Aqueous Solution as Studied by NMR

According to actual literature data, hyaluronic acid (HA) that is presented in the extracellular matrix can interact with proteins and thereby affect several important functions of the cell membrane. The purpose of this work was to reveal the features of the interaction of HA with proteins using the PFG NMR method by sampling two systems: aqueous solutions of HA with bovine serum albumin (BSA) and aqueous solutions of HA with hen egg-white lysozyme (HEWL). It was found that the presence of BSA...

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0 Replies | 214 Views
A methyl-TROSY based 13C relaxation dispersion NMR experiment for studies of chemical exchange in proteins
Apr 26, 2023 - 1:50 PM - by nmrlearner
nmrlearner's Avatar A methyl-TROSY based 13C relaxation dispersion NMR experiment for studies of chemical exchange in proteins

Abstract

A methyl Transverse Relaxation Optimized Spectroscopy (methyl-TROSY) based, multiple quantum (MQ) 13C Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion NMR experiment is described. The experiment is derived from the previously developed MQ 13Cā??1H CPMG scheme (Korzhnev in J Am Chem Soc 126: 3964ā??73, 2004) supplemented with a CPMG train of refocusing 1H pulses applied with constant frequency and synchronized with the 13C CPMG pulse train. The optimal 1H ā??decouplingā?? scheme that minimizes the amount of fast-relaxing methyl MQ magnetization present during CPMG intervals, makes use of an XY-4 phase cycling of the refocusing composite 1H pulses. For small-to-medium sized proteins, the MQ 13C CPMG experiment has the advantage over its single quantum (SQ) 13C counterpart of significantly reducing intrinsic, exchange-free relaxation rates of methyl coherences. For high molecular weight proteins, the MQ 13C CPMG experiment eliminates complications in the interpretation of MQ 13Cā??1H CPMG relaxation dispersion profiles arising from contributions to exchange from differences in methyl 1H chemical shifts between ground and excited states. The MQ 13C CPMG experiment is tested on two protein systems: (1) a triple mutant of the Fyn SH3 domain that interconverts slowly on the chemical shift time scale between the major folded state and an excited state folding intermediate; and (2) the 82-kDa enzyme Malate Synthase G (MSG), where chemical exchange at individual Ile Ī“1 methyl positions occurs on a much faster time-scale.



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[NMR paper] A methyl-TROSY based 13C relaxation dispersion NMR experiment for studies of chemical exchange in proteins
Apr 25, 2023 - 1:59 PM - by nmrlearner
nmrlearner's Avatar A methyl-TROSY based 13C relaxation dispersion NMR experiment for studies of chemical exchange in proteins

A methyl Transverse Relaxation Optimized Spectroscopy (methyl-TROSY) based, multiple quantum (MQ) ^(13)C Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion NMR experiment is described. The experiment is derived from the previously developed MQ ^(13)C-¹H CPMG scheme (Korzhnev in J Am Chem Soc 126: 3964-73, 2004) supplemented with a CPMG train of refocusing ¹H pulses applied with constant frequency and synchronized with the ^(13)C CPMG pulse train. The optimal ¹H 'decoupling' scheme that...

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0 Replies | 188 Views
[NMR paper] NMR detection and conformational dependence of two, three, and four-bond isotope shifts due to deuteration of backbone amides
Apr 25, 2023 - 1:59 PM - by nmrlearner
nmrlearner's Avatar NMR detection and conformational dependence of two, three, and four-bond isotope shifts due to deuteration of backbone amides

NMR isotope shifts occur due to small differences in nuclear shielding when nearby atoms are different isotopes. For molecules dissolved in 1:1 H(2)O:D(2)O, the resulting mixture of N-H and N-D isotopes leads to a small splitting of resonances from adjacent nuclei. We used multidimensional NMR to measure isotope shifts for the proteins CUS-3iD and CspA. We observed four-bond ??N(ND) isotope shifts in high-resolution 2D ^(15)N-TROSY experiments of the perdeuterated proteins that correlate with...

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0 Replies | 175 Views
[NMR paper] Characterizing the monomer-dimer equilibrium of UbcH8/Ube2L6: A combined SAXS and NMR study
Apr 25, 2023 - 1:59 PM - by nmrlearner
nmrlearner's Avatar Characterizing the monomer-dimer equilibrium of UbcH8/Ube2L6: A combined SAXS and NMR study

Interferon-stimulated gene-15 (ISG15) is an interferon-induced protein with two ubiquitin-like (Ubl) domains linked by a short peptide chain, and the conjugated protein of the ISGylation system. Similar to ubiquitin and other Ubls, ISG15 is ligated to its target proteins with a series of E1, E2, and E3 enzymes known as Uba7, Ube2L6/UbcH8, and HERC5, respectively. Ube2L6/UbcH8 plays a literal central role in ISGylation, underscoring it as an important drug target for boosting innate antiviral...

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0 Replies | 185 Views
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