density prior to induction of toxic target protein Soluble protein ...
22/04/2014 3:22:09 AM GMT
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NMR investigations of metal interactions with unstructured soluble protein domains
NMR investigations of metal interactions with unstructured soluble protein domains
Publication date: Available online 28 February 2014
Source:Coordination Chemistry Reviews</br>
Author(s): Riccardo De Ricco , Slawomir Potocki , Henryk Kozlowski , Daniela Valensin</br>
Essential main-group elements and transition metal ions play key roles in the structural organization and biological function of many macromolecules such as proteins, DNA, and RNA. Healthy conditions require tight regulation of metal concentrations inside and outside cells, and both metal...
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02-28-2014 07:08 PM
[NMR paper] NMR Spectroscopy of Soluble Protein Complexes at One Mega-Dalton and Beyond.
NMR Spectroscopy of Soluble Protein Complexes at One Mega-Dalton and Beyond.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles NMR Spectroscopy of Soluble Protein Complexes at One Mega-Dalton and Beyond.
Angew Chem Int Ed Engl. 2013 Jul 19;
Authors: Mainz A, Religa TL, Sprangers R, Linser R, Kay LE, Reif B
Abstract
Bigger is better: Sequential backbone assignments are obtained by NMR spectroscopy for a 1 MDa proteasome...
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07-23-2013 09:52 PM
[NMR paper] Using a Fragment-Based Approach To Target Protein-Protein Interactions.
Using a Fragment-Based Approach To Target Protein-Protein Interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2251-04-WileyOnlineLibrary-Button_120x27px_FullTextFree.gif Related Articles Using a Fragment-Based Approach To Target Protein-Protein Interactions.
Chembiochem. 2013 Jan 23;
Authors: Scott DE, Ehebauer MT, Pukala T, Marsh M, Blundell TL, Venkitaraman AR, Abell C, Hyvönen M
...
[Question from NMRWiki Q&A forum] Observing protein-ligand interaction using weakly soluble compounds
Observing protein-ligand interaction using weakly soluble compounds
I am trying to setup an experiment using HSQC with titration of a compound to determine the Kd of the protein-ligand interaction. My difficulties have been in the sample preparation/formulation, as these novel compounds are very weakly soluble in aqueous buffers. I must be able to quantify the soluble concentration of compound over ~6-8 points to generate the binding curve (signal intensity/chemical shift vs. ).
Previous observation of this protein by HSQC and other NMR techniques have used a buffer containing 5 mM...
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07-31-2012 08:27 PM
[NMR paper] Interaction of the water-soluble protein aprotinin with liposomes: gel-filtration, tu
Interaction of the water-soluble protein aprotinin with liposomes: gel-filtration, turbidity studies, and 31P NMR studies.
Related Articles Interaction of the water-soluble protein aprotinin with liposomes: gel-filtration, turbidity studies, and 31P NMR studies.
J Liposome Res. 2003 Nov;13(3-4):213-29
Authors: Tiourina O, Sharf T, Balkina A, Ollivon M, Selischeva A, Sorokoumova G, Larionova N
The interactions of a water-soluble nonmembrane protein aprotinin with multilamellar vesicles (MLV) and small unilamellar vesicles (SUV) from soybean...
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11-24-2010 09:16 PM
Efficient protein production method for NMR using soluble protein tags with cold shoc
Efficient protein production method for NMR using soluble protein tags with cold shock expression vector
Abstract The E. coli protein expression system is one of the most useful methods employed for NMR sample preparation. However, the production of some recombinant proteins in E. coli is often hampered by difficulties such as low expression level and low solubility. To address these problems, a modified cold-shock expression system containing a glutathione S-transferase (GST) tag, the pCold-GST system, was investigated. The pCold-GST system successfully expressed 9 out of 10 proteins...
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09-18-2010 04:53 AM
Efficient protein production method for NMR using soluble protein tags with cold shoc
Efficient protein production method for NMR using soluble protein tags with cold shock expression vector.
Related Articles Efficient protein production method for NMR using soluble protein tags with cold shock expression vector.
J Biomol NMR. 2010 Sep 16;
Authors: Hayashi K, Kojima C
The E. coli protein expression system is one of the most useful methods employed for NMR sample preparation. However, the production of some recombinant proteins in E. coli is often hampered by difficulties such as low expression level and low solubility. To...