Available online 11 January 2013
Publication year: 2013 Source:FEBS Letters
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 characterized by in-cell NMR, and then discuss the remaining challenges and future directions.
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...
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On-Cell MAS NMR: PhysiologicalClues from Living Cells
On-Cell MAS NMR: PhysiologicalClues from Living Cells
Giorgia Zandomeneghi, Karin Ilg, Markus Aebi and Beat H. Meier
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja307467p/aop/images/medium/ja-2012-07467p_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja307467p
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10-15-2012 10:49 PM
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
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Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
J Am Chem Soc. 2010 Dec 27;
Authors: Esadze A, Li DW, Wang T, Bru?schweiler R, Iwahara J
Despite their importance in macromolecular interactions and functions, the dynamics of lysine side-chain amino groups in proteins are not well understood. In this study, we have developed the methodology for the investigations of the dynamics...
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12-29-2010 04:04 PM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Alexandre Esadze, Da-Wei Li, Tianzhi Wang, Rafael Bru?schweiler and Junji Iwahara
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107847d/aop/images/medium/ja-2010-07847d_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107847d
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Protein dynamics in living cells studied by in-cell NMR spectroscopy
Linear Mode
