Protein-Protein Compounds - The Flip Side - Corante
Protein-Protein Compounds - The Flip Side - Corante
Protein-Protein Compounds - The Flip Side Corante
You'd probably be able to see this effect by biophysical techniques as well - NMR, SPR (if you could recapitulate the protein-protein interaction with an immobilized partner on a chip), etc. You'd want a lot of structural information - seeing some sort ...
Single-Cell NMR? How About Single-Protein NMR? - Corante
Single-Cell NMR? How About Single-Protein NMR? - Corante
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Single-Cell NMR? How About Single-Protein NMR?
Corante
Two different research teams have reported a completely different way to run NMR experiments, one that looks like it could take the resolution down to cellular (or even large protein) levels. These two papers in Science have the details (and there's an ...
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02-04-2013 08:00 PM
[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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News from other NMR forums
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07-31-2012 08:27 PM
Advancing fragment binders to lead-like compounds using ligand and protein-based NMR spectroscopy.
Advancing fragment binders to lead-like compounds using ligand and protein-based NMR spectroscopy.
Advancing fragment binders to lead-like compounds using ligand and protein-based NMR spectroscopy.
Methods Enzymol. 2011;493:469-85
Authors: Maurer T
The application of NMR in fragment-based lead discovery (FBLD) has quickly developed from a sensitive method for the identification of low-affinity binders to an important tool in the hit-to-lead process. NMR can play a constructive role in the process from identifying those fragments with the best...
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Protein Pept Lett. 2011 Jan 11;
Authors: Yang D
Protein side chain dynamics is associated with protein stability, folding, and intermolecular interactions. Detailed dynamics information is crucial for the understanding of protein function and biochemical and biophysical properties, which can be obtained using NMR relaxation techniques. In this review, (13)C relaxation of methine, methylene and methyl groups with and without...
nmrlearner
Journal club
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01-13-2011 12:00 PM
[NMR paper] What contributions to protein side-chain dynamics are probed by NMR experiments? A mo
What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.
Related Articles What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.
J Mol Biol. 2005 May 27;349(1):185-203
Authors: Best RB, Clarke J, Karplus M
Molecular dynamics simulations of the structurally homologous proteins TNfn3 and FNfn10 have been used to investigate the contributions to side-chain dynamics measured by NMR relaxation experiments. The...
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Journal club
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11-24-2010 11:14 PM
[NMR paper] Use of selective Trp side chain labeling to characterize protein-protein and protein-
Use of selective Trp side chain labeling to characterize protein-protein and protein-ligand interactions by NMR spectroscopy.
Related Articles Use of selective Trp side chain labeling to characterize protein-protein and protein-ligand interactions by NMR spectroscopy.
J Am Chem Soc. 2003 Mar 12;125(10):2892-3
Authors: Rodriguez-Mias RA, Pellecchia M
Recent studies on amino acid occurrence in protein binding sites suggest that only a reduced number of residues are responsible for most interaction energy in protein-protein and protein-ligand...