3D structure determination of a protein in living cells using paramagnetic NMR spectroscopy.
Chem Commun (Camb). 2016 Jul 29;
Authors: Pan BB, Yang F, Ye Y, Wu Q, Li C, Huber T, Su XC
Abstract
Determining the three-dimensional structure of a protein in living cells remains particularly challenging. We demonstrated that the integration of site-specific tagging proteins and GPS-Rosetta calculations provides a fast and effective way of determining the structures of proteins in living cells, and in principle the interactions and dynamics of protein-ligand complexes.
PMID: 27470136 [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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[NMR paper] Protein Structure Determination with Paramagnetic Solid-State NMR Spectroscopy.
Protein Structure Determination with Paramagnetic Solid-State NMR Spectroscopy.
Related Articles Protein Structure Determination with Paramagnetic Solid-State NMR Spectroscopy.
Acc Chem Res. 2013 Mar 6;
Authors: Sengupta I, Nadaud PS, Jaroniec CP
Abstract
Many structures of the proteins and protein assemblies that play central roles in fundamental biological processes and disease pathogenesis are not readily accessible via the conventional techniques of single-crystal X-ray diffraction and solution-state nuclear magnetic resonance (NMR)....
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03-08-2013 10:35 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...
3D structure determination of a protein in living cells using paramagnetic NMR spectroscopy.
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