Glycogen is a readily deployed intracellular energy storage macromolecule composed of branched chains of glucose anchored to the protein glycogenin. Although glycogen primarily occurs in the liver and muscle, it is found in most tissues, and its metabolism has been shown to be important in cancers and immune cells. Robust analysis of glycogen turnover requires stable isotope tracing plus a reliable means of quantifying total and labeled glycogen derived from precursors such as ^(13)C(6)-glucose....
[ASAP] Exposing the Interplay Between Enzyme Turnover, Protein Dynamics, and the Membrane Environment in Monoamine Oxidase B
Exposing the Interplay Between Enzyme Turnover, Protein Dynamics, and the Membrane Environment in Monoamine Oxidase B
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b00213/20190423/images/medium/bi-2019-00213b_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b00213
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[NMR paper] Micro-scale NMR Experiments for Monitoring the Optimization of Membrane Protein Solutions for Structural Biology.
Micro-scale NMR Experiments for Monitoring the Optimization of Membrane Protein Solutions for Structural Biology.
Micro-scale NMR Experiments for Monitoring the Optimization of Membrane Protein Solutions for Structural Biology.
Bio Protoc. 2015 Jul 20;5(14)
Authors: Horst R, Wüthrich K
Abstract
Reconstitution of integral membrane proteins (IMP) in aqueous solutions of detergent micelles has been extensively used in structural biology, using either X-ray crystallography or NMR in solution. Further progress could be achieved by...
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04-15-2016 05:06 PM
[NMR paper] The micro-scale synthesis of (117)Sn-enriched tributyltin chloride and its characterization by GC-ICP-MS and NMR techniques.
The micro-scale synthesis of (117)Sn-enriched tributyltin chloride and its characterization by GC-ICP-MS and NMR techniques.
Related Articles The micro-scale synthesis of (117)Sn-enriched tributyltin chloride and its characterization by GC-ICP-MS and NMR techniques.
Chemosphere. 2014 Jan 25;
Authors: Peeters K, Iskra J, Zuliani T, S?an?ar J, Mila?i? R
Abstract
Organotin compounds (OTCs) are among the most toxic substances ever introduced to the environment by man. They are common pollutants in marine ecosystems, but are also present in the...
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01-30-2014 05:38 PM
[NMR paper] SOS-NMR: a saturation transfer NMR-based method for determining the structures of pro
SOS-NMR: a saturation transfer NMR-based method for determining the structures of protein-ligand complexes.
Related Articles SOS-NMR: a saturation transfer NMR-based method for determining the structures of protein-ligand complexes.
J Am Chem Soc. 2004 Mar 3;126(8):2390-8
Authors: Hajduk PJ, Mack JC, Olejniczak ET, Park C, Dandliker PJ, Beutel BA
An NMR-based alternative to traditional X-ray crystallography and NMR methods for structure-based drug design is described that enables the structure determination of ligands complexed to virtually...
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11-24-2010 09:25 PM
[NMR paper] A general method for determining the electron self-exchange rates of blue copper prot
A general method for determining the electron self-exchange rates of blue copper proteins by longitudinal NMR relaxation.
Related Articles A general method for determining the electron self-exchange rates of blue copper proteins by longitudinal NMR relaxation.
J Am Chem Soc. 2002 Apr 17;124(15):4093-6
Authors: Jensen MR, Hansen DF, Led JJ
A general NMR method is presented that allows a precise determination of the second-order rate constant, k(ese), for the electron self-exchange in blue copper proteins, from the longitudinal relaxation...
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[NMR paper] A novel NMR method for determining the interfaces of large protein-protein complexes.
A novel NMR method for determining the interfaces of large protein-protein complexes.
Related Articles A novel NMR method for determining the interfaces of large protein-protein complexes.
Nat Struct Biol. 2000 Mar;7(3):220-3
Authors: Takahashi H, Nakanishi T, Kami K, Arata Y, Shimada I
Identification of the interfaces of large (Mr > 50,000) protein-protein complexes in solution by high resolution NMR has typically been achieved using experiments involving chemical shift perturbation and/or hydrogen-deuterium exchange of the main chain amide...
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[NMR paper] The button test: a small scale method using microdialysis cells for assessing protein
The button test: a small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMR.
Related Articles The button test: a small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMR.
J Biomol NMR. 1997 Oct;10(3):279-82
Authors: Bagby S, Tong KI, Liu D, Alattia JR, Ikura M
A simple method has been developed for screening solution conditions to determine conditions under which a protein is soluble at the high concentrations typically used for NMR...
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HIFI-C: a robust and fast method for determining NMR couplings from adaptive 3D to 2D projections
HIFI-C: a robust and fast method for determining NMR couplings from adaptive 3D to 2D projections
Gabriel Cornilescu, Arash Bahrami, Marco Tonelli, John L. Markley and Hamid R. Eghbalnia
Journal of Biomolecular NMR; 2007; 38(4); pp 341-351
Abstract:
We describe a novel method for the robust, rapid, and reliable determination of J couplings in multi-dimensional NMR coupling data, including small couplings from larger proteins. The method, “High-resolution Iterative Frequency Identification of Couplings” (HIFI-C) is an extension of the adaptive and intelligent data collection approach...
A Micro-Scale Analytical Method for Determining Glycogen Turnover by NMR and FTMS
Linear Mode
