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[NMR paper] (1)H nuclear magnetic resonance (NMR)-based serum metabolomics of human gallbladder inflammation.
May 24, 2017 - 7:40 PM - by nmrlearner
nmrlearner's Avatar (1)H nuclear magnetic resonance (NMR)-based serum metabolomics of human gallbladder inflammation.

Related Articles (1)H nuclear magnetic resonance (NMR)-based serum metabolomics of human gallbladder inflammation.

Inflamm Res. 2017 Jan;66(1):97-105

Authors: Sharma RK, Mishra K, Farooqui A, Behari A, Kapoor VK, Sinha N

Abstract
OBJECTIVE AND DESIGN: We present in this article (1)H nuclear magnetic resonance (NMR)-based metabolic approach to screen the serum metabolic alterations in human gallbladder inflammation with chronic cholecystitis (CC).
MATERIAL/METHODS: Total of 71 human serum samples was divided into two groups, (n*=*41, CC) and (n*=*30 control). (1)H NMR metabolic profiling was carried out for investigation of metabolic alterations. Multivariate statistical analysis was applied for pattern recognition and identification of metabolites playing crucial role in gallbladder inflammation. Receiver operating curve (ROC) and pathway analysis on NMR data were also carried out to validate the findings.
RESULTS: Serum... [Read More]
0 Replies | 38 Views
[NMR paper] Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies.
May 24, 2017 - 7:40 PM - by nmrlearner
nmrlearner's Avatar Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies.

Related Articles Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies.

Arch Biochem Biophys. 2016 Sep 15;606:81-9

Authors: Yang H, Huang Y, He J, Li S, Tang B, Li H

Abstract
In this study, lafutidine (LAF) was used as a model compound to investigate the binding mechanism between antiulcer drugs and human serum albumin (HSA) through various techniques, including STD-NMR, WaterLOGSY-NMR, (1)H NMR relaxation times, tr-NOESY, molecule docking calculation, FT-IR spectroscopy, and CD spectroscopy. The analyses of STD-NMR, which derived relative STD (%) intensities, and WaterLOGSY-NMR, determined that LAF bound to HSA. In particular, the pyridyl group of LAF was in close contact with HSA binding pocket, whereas furyl... [Read More]
0 Replies | 67 Views
High field hyperpolarization-EXSY experiment for fast determination of dissociation rates in SABRE complexes
May 24, 2017 - 7:40 PM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

High field hyperpolarization-EXSY experiment for fast determination of dissociation rates in SABRE complexes

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Hermkens, N.K.J., et al., High field hyperpolarization-EXSY experiment for fast determination of dissociation rates in SABRE complexes. J. Magn. Reson., 2017. 276: p. 122-127.


https://doi.org/10.1016/j.jmr.2017.01.011


SABRE (Signal Amplification By Reversible Exchange) is a nuclear spin hyperpolarization technique based on the reversible concurrent binding of small molecules and para-hydrogen (p-H2) to an iridium metal complex in solution. At low magnetic field, spontaneous conversion of p-H2 spin order to enhanced longitudinal magnetization of the nuclear spins of the other ligands occurs. Subsequent complex dissociation results in hyperpolarized substrate molecules in solution. The lifetime of this complex plays a crucial role in attained SABRE NMR signal enhancements. Depending on the ligands, vastly different dissociation rates have been previously measured using EXSY or selective inversion experiments. However, both these approaches are generally time-consuming due to the long recycle delays (up to 2 min) necessary to reach thermal equilibrium for the nuclear spins of interest. In the cases of dilute solutions, signal averaging aggravates the problem, further extending the experimental time. Here, a new... [Read More]
0 Replies | 70 Views
Application of the Halogen Bond in Protein Systems
May 24, 2017 - 6:27 AM - by nmrlearner
nmrlearner's Avatar Application of the Halogen Bond in Protein Systems



Biochemistry
DOI: 10.1021/acs.biochem.7b00371



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0 Replies | 56 Views
NMR Analysis of Amide Hydrogen Exchange Rates in a Pentapeptide-Repeat Protein from A.*thaliana
May 23, 2017 - 4:45 PM - by nmrlearner
nmrlearner's Avatar NMR Analysis of Amide Hydrogen Exchange Rates in a Pentapeptide-Repeat Protein from A.*thaliana

Publication date: 23 May 2017
Source:Biophysical Journal, Volume 112, Issue 10

Author(s): Shenyuan Xu, Shuisong Ni, Michael A. Kennedy

At2g44920 from Arabidopsis thaliana is a pentapeptide-repeat protein (PRP) composed of 25 repeats capped by*N- and C-terminal ?-helices. PRP structures are dominated by four-sided right-handed ?-helices typically consisting of mixtures of type II and type IV ?-turns. PRPs adopt repeated five-residue (Rfr) folds with an Rfr consensus sequence (STAV)(D/N)(L/F)(S/T/R)(X). Unlike other PRPs, At2g44920 consists exclusively of type II ?-turns. At2g44920 is predicted to be located in the thylakoid lumen although its biochemical function remains unknown. Given its unusual structure, we investigated the biophysical properties of At2g44920 as a representative of the ?-helix family to determine if it had exceptional global stability, backbone dynamics, or amide hydrogen exchange rates. Circular dichroism measurements yielded a melting point of 62.8░C, indicating unexceptional global thermal stability. Nuclear spin relaxation measurements indicated that the Rfr-fold core was rigid with order parameters ranging from 0.7 to 0.9. At2g44920 exhibited a striking range of amide hydrogen exchange rates spanning 10 orders of magnitude, with lifetimes ranging from minutes to several months. A weak correlation was found among hydrogen... [Read More]
0 Replies | 39 Views
[NMR paper] Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR.
May 23, 2017 - 4:45 PM - by nmrlearner
nmrlearner's Avatar Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR.

Related Articles Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR.

J Phys Chem Lett. 2017 May 22;:

Authors: Ceccon A, Tugarinov V, Boughton AJ, Fushman D, Clore GM

Abstract
The interactions of two model multi-domain proteins - covalently linked di-ubiquitins, Ub2 - with lipid-based nanoparticles have been quantitatively probed by the measurements of NMR lifetime line broadening, ?R2. By combined analysis of ?R2 profiles arising from interactions with liposomes of varying sizes, an approach recently developed for the characterization of interactions of mono-ubiquitin with liposomes, we determine how the parameters of exchange (liposome binding) and dynamics of each individual domain of Ub2 on the surface of liposomes change when the domains are covalently attached to one another by a flexible linker. Two different covalent linkages were used: K63-linked and K48-linked Ub2. The possibility of three distinct modes of binding of Ub2 to liposomes requires the introduction of simple but important modifications to the strategy of analysis originally developed for mono-ubiquitin.


PMID: 28530812 [PubMed - as supplied by publisher]



... [Read More]
0 Replies | 45 Views
[NMR paper] Applications of NMR to membrane proteins.
May 23, 2017 - 4:45 PM - by nmrlearner
nmrlearner's Avatar Applications of NMR to membrane proteins.

Related Articles Applications of NMR to membrane proteins.

Arch Biochem Biophys. 2017 May 18;:

Authors: Opella SJ, Marassi FM

Abstract
Membrane proteins present a challenge for structural biology. In this article, we review some of the recent developments that advance the application of NMR to membrane proteins, with emphasis on structural studies in detergent-free, lipid bilayer samples that resemble the native environment. NMR spectroscopy is not only ideally suited for structure determination of membrane proteins in hydrated lipid bilayer membranes, but also highly complementary to the other principal techniques based on X-ray and electron diffraction. Recent advances in NMR instrumentation, spectroscopic methods, computational methods, and sample preparations are driving exciting new efforts in membrane protein structural biology.


PMID: 28529197 [PubMed - as supplied by publisher]



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0 Replies | 43 Views
Molecular dynamics-based selectivity for Fast-Field-Cycling relaxometry by Overhauser and solid effect dynamic nuclear polarization #DNPNMR
May 23, 2017 - 4:44 AM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

Molecular dynamics-based selectivity for Fast-Field-Cycling relaxometry by Overhauser and solid effect dynamic nuclear polarization #DNPNMR

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Neudert, O., C. Mattea, and S. Stapf, Molecular dynamics-based selectivity for Fast-Field-Cycling relaxometry by Overhauser and solid effect dynamic nuclear polarization. J. Magn. Reson., 2017. 276: p. 113-121.


http://www.sciencedirect.com/science...90780717300204


In the last decade nuclear spin hyperpolarization methods, especially Dynamic Nuclear Polarization (DNP), have provided unprecedented possibilities for various NMR techniques by increasing the sensitivity by several orders of magnitude. Recently, in-situ DNP-enhanced Fast Field Cycling (FFC) relaxometry was shown to provide appreciable NMR signal enhancements in liquids and viscous systems. In this work, a measurement protocol for DNP-enhanced NMR studies is introduced which enables the selective detection of nuclear spin hyperpolarized by either Overhauser effect or solid effect DNP. Based on field-cycled DNP and relaxation studies it is shown that these methods allow for the independent measurement of polymer and solvent nuclear spins in a concentrated solution of high molecular weight polybutadiene in benzene doped with ?,?-bisdiphenylene-?-phenylallyl radical. Appreciable NMR signal enhancements of about 10-fold were obtained for both constituents.... [Read More]
0 Replies | 60 Views
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