Diels-Alder reactionâ??triggered bioorthogonal protein decaging in living cells - Nature.com
Diels-Alder reactionâ??triggered bioorthogonal protein decaging in living cells - Nature.com
Diels-Alder reactionâ??triggered bioorthogonal protein decaging in living cells Nature.com
A generally applicable strategy, however, remains elusive. Herein we describe a small moleculeâ??triggered bioorthogonal protein decaging technique that relies on the inverse electron-demand Diels-Alder reaction for eliminating a chemically caged protein...
[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 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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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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High-Resolution HeteronuclearMultidimensional NMRof Proteins in Living Insect Cells Using a Baculovirus Protein ExpressionSystem
High-Resolution HeteronuclearMultidimensional NMRof Proteins in Living Insect Cells Using a Baculovirus Protein ExpressionSystem
Jumpei Hamatsu, Daniel O’Donovan, Takashi Tanaka, Takahiro Shirai, Yuichiro Hourai, Tsutomu Mikawa, Teppei Ikeya, Masaki Mishima, Wayne Boucher, Brian O. Smith, Ernest D. Laue, Masahiro Shirakawa and Yutaka Ito
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja310928u/aop/images/medium/ja-2012-10928u_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja310928u...