Functional Binding Surface of a ?-Hairpin VEGF Receptor Targeting Peptide Determined by NMR Spectroscopy in Living Cells.
Chemistry. 2014 Nov 6;
Authors: Diana D, Russomanno A, Rosa LD, Di Stasi R, Capasso D, Di Gaetano S, Romanelli A, Russo L, D'Andrea LD, Fattorusso R
Abstract
In this study, the functional interaction of HPLW peptide with VEGFR2 (Vascular Endothelial Growth Factor Receptor 2) was determined by using fast (15) N-edited NMR spectroscopic experiments. To this aim, (15) N uniformly labelled HPLW has been added to Porcine Aortic Endothelial Cells. The acquisition of isotope-edited NMR spectroscopic experiments, including (15) N relaxation measurements, allowed a precise characterization of the in-cell HPLW epitope recognized by VEGFR2.
PMID: 25378243 [PubMed - as supplied by publisher]
[NMR paper] (19) F NMR Spectroscopy as a Probe of Cytoplasmic Viscosity and Weak Protein Interactions in Living Cells.
(19) F NMR Spectroscopy as a Probe of Cytoplasmic Viscosity and Weak Protein Interactions in Living Cells.
(19) F NMR Spectroscopy as a Probe of Cytoplasmic Viscosity and Weak Protein Interactions in Living Cells.
Chemistry. 2013 Aug 6;
Authors: Ye Y, Liu X, Zhang Z, Wu Q, Jiang B, Jiang L, Zhang X, Liu M, Pielak GJ, Li C
Abstract
Protein mobility in living cells is vital for cell function. Both cytosolic viscosity and weak protein-protein interactions affect mobility, but examining viscosity and weak interaction effects is challenging....
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08-08-2013 03:46 PM
[NMR paper] Protein dynamics in living cells studied by in-cell NMR spectroscopy.
Protein dynamics in living cells studied by in-cell NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein dynamics in living cells studied by in-cell NMR spectroscopy.
FEBS Lett. 2013 Jan 11;
Authors: Li C, Liu M
Abstract
Most proteins function in cells where protein concentrations can reach 400g/l. However, most quantitative studies of protein properties are performed in idealized, dilute conditions. Recently developed in-cell NMR techniques...
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02-03-2013 10:22 AM
Protein dynamics in living cells studied by in-cell NMR spectroscopy
Protein dynamics in living cells studied by in-cell NMR spectroscopy
Available online 11 January 2013
Publication year: 2013
Source:FEBS Letters</br>
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Most proteins function in cells where protein concentrations can reach 400g/l. However, most quantitative studies of protein properties are performed in idealized, dilute conditions. Recently developed in-cell NMR techniques can provide protein structure and other biophysical properties inside living cells at atomic resolution. Here we review how protein dynamics, including global and internal motions have been...
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02-03-2013 10:13 AM
Watching protein structure at work in living cells using NMR spectroscopy
Watching protein structure at work in living cells using NMR spectroscopy
December 2012
Publication year: 2012
Source:Current Opinion in Chemical Biology, Volume 16, Issues 5–6</br>
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Isotope-assisted multi-dimensional NMR spectroscopy can now be applied to proteins inside living cells. The technique, called in-cell NMR, aims to investigate the structures, interactions and dynamics of proteins under their native conditions, ideally at an atomic resolution. The application has begun with bacterial cells but has now expanded to mammalian cultured cells, such as HeLa...
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02-03-2013 10:13 AM
STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells.
STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells.
STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells.
Chembiochem. 2011 Mar 21;12(5):695-9
Authors: Potenza D, Vasile F, Belvisi L, Civera M, Araldi EM
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07-19-2011 07:52 PM
13C direct-detection biomolecular NMR spectroscopy in living cells.
13C direct-detection biomolecular NMR spectroscopy in living cells.
13C direct-detection biomolecular NMR spectroscopy in living cells.
Angew Chem Int Ed Engl. 2011 Mar 1;50(10):2339-41
Authors: Bertini I, Felli IC, Gonnelli L, Kumar M V V, Pierattelli R
Functional Binding Surface of a ?-Hairpin VEGF Receptor Targeting Peptide Determined by NMR Spectroscopy in Living Cells.
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