Process and Reaction Monitoring by Low-Field NMR Spectroscopy
Process and Reaction Monitoring by Low-Field NMR Spectroscopy
Publication year: 2011
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, Available online 6 December 2011</br>
Franz*Dalitz, Markus*Cudaj, Michael*Maiwald, Gisela*Guthausen</br>
http://www.sciencedirect.com/cache/MiamiImageURL/1-s2.0-S0079656511000860-fx1.sml</br></br></br>
More...
nmrlearner
Journal club
0
12-07-2011 08:26 AM
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
J Phys Chem B. 2011 May 2;
Authors: Hwang S, Shao Q, Williams H, Hilty C, Gao YQ
A combined simulation and experimental study was performed to investigate how methanol affects the structure of a model peptide BBA5. BBA5 forms a stable ?-hairpin-?-helix structure in aqueous solutions....
nmrlearner
Journal club
0
05-04-2011 04:14 PM
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
J Biol Inorg Chem. 2011 Apr 3;
Authors: Teixeira JM, Dias DM, Cañada FJ, Martins JA, André JP, Jiménez-Barbero J, Geraldes CF
The study of ligand-receptor interactions using high-resolution NMR techniques, namely the saturation transfer difference (STD),...
nmrlearner
Journal club
0
04-05-2011 10:22 PM
[NMR paper] Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
Related Articles Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
J Am Chem Soc. 2005 Aug 24;127(33):11676-83
Authors: Desvaux H, Dubois L, Huber G, Quillin ML, Berthault P, Matthews BW
Wild-type bacteriophage T4 lysozyme contains a hydrophobic cavity with binding properties that have been...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR
Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR correlation spectra.
Related Articles Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR correlation spectra.
J Biomol NMR. 2003 Mar;25(3):217-23
Authors: van Rossum BJ, Castellani F, Pauli J, Rehbein K, Hollander J, de Groot HJ, Oschkinat H
In this paper, we present a strategy for the (1)H(N) resonance assignment in solid-state magic-angle spinning (MAS) NMR, using the alpha-spectrin SH3 domain as an example. A novel 3D...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[NMR paper] 19F NMR magnetization transfer between 5-FBAPTA and its complexes. An alternative mea
19F NMR magnetization transfer between 5-FBAPTA and its complexes. An alternative means for measuring free Ca2+ concentration, and detection of complexes with protein in erythrocytes.
Related Articles 19F NMR magnetization transfer between 5-FBAPTA and its complexes. An alternative means for measuring free Ca2+ concentration, and detection of complexes with protein in erythrocytes.
NMR Biomed. 1994 Nov;7(7):330-8
Authors: Gilboa H, Chapman BE, Kuchel PW
The 19F NMR Ca(2+)-indicator molecule 5,5'-difluoro-1,2-bis(o-...
nmrlearner
Journal club
0
08-22-2010 03:29 AM
[NMR paper] Proton-transfer effects in the active-site region of Escherichia coli thioredoxin usi
Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.
Related Articles Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.
Biochemistry. 1991 Apr 30;30(17):4262-8
Authors: Dyson HJ, Tennant LL, Holmgren A
A series of two-dimensional (2D) correlated 1H NMR spectra of reduced and oxidized Escherichia coli thioredoxin have been used to probe the effects of pH in the vicinity of the active site, -Cys32-Gly-Pro-Cys35-, using the...