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» Online Users: 22 |
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| Most users ever online was 99, 08-22-2010 at 11:14 AM. |
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 Postdoctoral Research Fellow |
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Sep 03, 2010 - 4:16 PM - by nmrlearner
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Postdoctoral Research Fellow
A Postdoctoral research position in Structural Biology is available to work on an NH&MRC funded project investigating the structure and interaction partners of tetraspanin-2 from the human parasite Schistosoma mansoni. This protein has been shown to be an effective vaccine target against schistosomiasis and will enter Phase I clinical trials in 2011. The position will be a joint appointment in the NMR Spectroscopy group at the Institute for Molecular Biosciences and the Queensland Tropical H…
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[NMR software blog] Oh, Sugar |
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Sep 03, 2010 - 4:16 PM - by nmrlearner
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Oh, Sugar
I have good news! With a minimal simplification of my INADEQUATE filter I have been able to rescue the last cross-peak of cholesterol. It had been rejected because too near to the diagonal. I changed the code saying: "if it's on the diagonal, it is bad; if it's just near, let's accept it". So it is possible to have the perfect INADEQUATE of cholesterol, with all the expected cross-peaks IN and everything else OUT.
Yesterday I received another INADEQUATE spectrum, this time of sucrose. The S/N is still high enough to make my filter unnecessary. If I play with the contour plot all the noise disappears while the 12 carbon atoms and their 10 bonds remain. Only a spurious peak remains at the coordinates 103.7;-22.9. I have not received the 1-D external projection, so I created it artificially. The spectral width is the same in both dimension (instead of being doubled for the DQF axis). The consequence is that two cross-peaks fall just on the boundary and are partially folded. This is the spectrum:
I have applied the filter with the same parameters used for the cholesterol (C-C coupling; linewidths in the two dimensions) while the threshold corresponds to the above plot. The result is perfect. All the cross-peaks are resolved and they are all present. Nothing else survives.
... [Read More]
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Application of NMR Spectroscopy in Medicinal Chemistry and Drug Discovery. |
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Sep 03, 2010 - 2:30 PM - by nmrlearner
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Application of NMR Spectroscopy in Medicinal Chemistry and Drug Discovery.
Related Articles Application of NMR Spectroscopy in Medicinal Chemistry and Drug Discovery.
Curr Top Med Chem. 2010 Sep 2;
Authors: Ohno A, Inomata K, Tochio H, Shirakawa M
"In-cell nuclear magnetic resonance (NMR)" is a unique method for characterization of conformation, interaction and dynamics of proteins inside living cells at atomic level. Since the method was proposed by Dötch and co-workers in 2001 [1], its application had been limited to bacterial cells and oocytes of Xenopus laevis [2]. Recently, we reported a method for efficient delivery of (15)N-labeled proteins into human HeLa cells using cell-penetrating peptides, and measured high-resolution two-dimensional (1)H-(15)N correlation spectra of proteins in the cells. The in-cell NMR spectroscopy in human cells is capable of analyzing structures, interactions, dynamics and stability of proteins inside cells. Of its possible applications, we propose that in-cell NMR spectroscopy can be utilized as an effective step in protein-targeted drug development process, by demonstrating that interaction of FKBP12 with immunosuppressants administered extracellularly was successfully observed in living cells. This observation suggests that drug delivery and capability of target proteins inside cells for interaction... [Read More]
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0 Replies | 1 Views
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NMR Screening and Hit Validation in Fragment Based Drug Discovery. |
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Sep 03, 2010 - 2:30 PM - by nmrlearner
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NMR Screening and Hit Validation in Fragment Based Drug Discovery.
Related Articles NMR Screening and Hit Validation in Fragment Based Drug Discovery.
Curr Top Med Chem. 2010 Sep 2;
Authors: Campos-Olivas R
Over the past three decades nuclear magnetic resonance spectroscopy has been developed into a mature technique for the characterization of interactions of small molecule ligands with their corresponding protein and nucleic acid receptors. In fact, a significant number of industrial and academic laboratories employ NMR for screening small molecule compound collections for binding to defined macromolecular targets, thus potentially providing initial, low affinity hits for a fragment-based approach in the drug discovery process. NMR is also applied to interrogate hits obtained by high throughput screening using biochemical assays and by virtual screening methods, for their ability to physically interact with the target receptor. In favorable cases a variety of NMR-based methods can also provide essential information to validate the hit, rank the different hits according to affinity, and to structurally analyze the ligand-target complex, thus providing essential information for structure-based optimization and medicinal chemistry. In this review a comprehensive overview of the large variety of NMR methods to study interactions between... [Read More]
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0 Replies | 1 Views
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Insights into the Mechanism of Ligand Binding to Octopine Dehydrogenase from Pecten m |
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Sep 03, 2010 - 2:30 PM - by nmrlearner
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Insights into the Mechanism of Ligand Binding to Octopine Dehydrogenase from Pecten maximus by NMR and Crystallography.
Related Articles Insights into the Mechanism of Ligand Binding to Octopine Dehydrogenase from Pecten maximus by NMR and Crystallography.
PLoS One. 2010;5(8):
Authors: Smits SH, Meyer T, Mueller A, van Os N, Stoldt M, Willbold D, Schmitt L, Grieshaber MK
Octopine dehydrogenase (OcDH) from the adductor muscle of the great scallop, Pecten maximus, catalyzes the NADH dependent, reductive condensation of L-arginine and pyruvate to octopine, NAD(+), and water during escape swimming and/or subsequent recovery. The structure of OcDH was recently solved and a reaction mechanism was proposed which implied an ordered binding of NADH, L-arginine and finally pyruvate. Here, the order of substrate binding as well as the underlying conformational changes were investigated by NMR confirming the model derived from the crystal structures. Furthermore, the crystal structure of the OcDH/NADH/agmatine complex was determined which suggests a key role of the side chain of L-arginine in protein cataylsis. Thus, the order of substrate binding to OcDH as well as the molecular signals involved in octopine formation can now be described in molecular detail.
PMID: 20808820 [PubMed - in process]
... [Read More]
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Faculty (Tenure Track) - University of Utah - Salt Lake City, UT, United States |
Sep 03, 2010 - 4:11 AM - by nmrlearner
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Faculty (Tenure Track) - University of Utah - Salt Lake City, UT, United States
CHEMISTRY, UNIVERSITY OF UTAH. Two tenure track positions are available in the general area of physical chemistry. Theory/computation, materials, and NMR are specific areas of interest, as are other interdisciplinary research areas. While the openings are at the Assistant Professor level, exceptional senior candidates may be considered. Candida...
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0 Replies | 4 Views
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Characterization of (1)H NMR signal in human cortical bone for magnetic resonance ima |
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Sep 02, 2010 - 3:58 PM - by nmrlearner
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Characterization of (1)H NMR signal in human cortical bone for magnetic resonance imaging.
Characterization of (1)H NMR signal in human cortical bone for magnetic resonance imaging.
Magn Reson Med. 2010 Sep;64(3):680-7
Authors: Horch RA, Nyman JS, Gochberg DF, Dortch RD, Does MD
Recent advancements in MRI have enabled clinical imaging of human cortical bone, providing a potentially powerful new means for assessing bone health with molecular-scale sensitivities unavailable to conventional X-ray-based diagnostics. In human cortical bone, MRI is sensitive to populations of protons ((1)H) partitioned among water and protein sources, which may be differentiated according to intrinsic NMR properties such as chemical shift and transverse and longitudinal relaxation rates. Herein, these NMR properties were assessed in human cortical bone donors from a broad age range, and four distinct (1)H populations were consistently identified and attributed to five microanatomical sources. These findings show that modern human cortical bone MRI contrast will be dominated by collagen-bound water, which can also be exploited to study human cortical bone collagen via magnetization transfer. Magn Reson Med, 2010. (c) 2010 Wiley-Liss, Inc.
PMID: 20806375 [PubMed - in process]
Source: ... [Read More]
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