Related ArticlesDetecting Intracellular Cysteine Redox States by in-Cell NMR Spectroscopy.
Chembiochem. 2013 Jul 24;
Authors: Silvers R, Schwalbe H
Abstract
An in-cell perspective: Nowadays, in-cell NMR spectroscopy has proven to be a thrilling alternative for the investigation of biomacromolecules under physiological conditions at atomic resolution. A recent example demonstrating significant progress in in-cell NMR was published by the groups of Banci and Aricescu that investigated the post-translational maturation of human superoxide dismutase 1 (SOD1) in living human cells.
PMID: 23893841 [PubMed - as supplied by publisher]
In-cell NMR spectroscopy
In-cell NMR spectroscopy
October 2011
Publication year: 2011
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 59, Issue 3</br>
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12-15-2012 09:51 AM
Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy
Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy
Abstract Cytochrome c (Cc) is a soluble electron carrier protein, transferring reducing equivalents between Cc reductase and Cc oxidase in eukaryotes. In this work, we assessed the structural differences between reduced and oxidized Cc in solution by paramagnetic NMR spectroscopy. First, we have obtained nearly-complete backbone NMR resonance assignments for iso-1-yeast Cc and horse Cc in both oxidation states. These were further used to derive pseudocontact shifts (PCSs) arising...
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02-13-2012 02:34 AM
Pb-207 NMR Spectroscopy Reveals that Pb(II) Coordinates with Glutathione (GSH) and Tris Cysteine Zinc Finger Proteins in a PbS(3) Coordination Environment.
Pb-207 NMR Spectroscopy Reveals that Pb(II) Coordinates with Glutathione (GSH) and Tris Cysteine Zinc Finger Proteins in a PbS(3) Coordination Environment.
Pb-207 NMR Spectroscopy Reveals that Pb(II) Coordinates with Glutathione (GSH) and Tris Cysteine Zinc Finger Proteins in a PbS(3) Coordination Environment.
J Inorg Biochem. 2011 Aug 1;105(8):1030-1034
Authors: Neupane KP, Pecoraro VL
(207)Pb NMR spectroscopy can be used to monitor the binding of Pb(II) to thiol rich biological small molecules such as glutathione and to zinc finger proteins. The...
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06-01-2011 02:30 PM
[NMR paper] In-cell NMR spectroscopy.
In-cell NMR spectroscopy.
Related Articles In-cell NMR spectroscopy.
Methods Enzymol. 2005;394:17-41
Authors: Serber Z, Corsini L, Durst F, Dötsch V
The role of a protein inside a cell is determined by both its location and its conformational state. Although fluorescence techniques are widely used to determine the cellular localization of proteins in vivo, these approaches cannot provide detailed information about a protein's three-dimensional state. This gap, however, can be filled by NMR spectroscopy, which can be used to investigate both...
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11-24-2010 11:14 PM
[NMR paper] Mutational analysis and NMR spectroscopy of quail cysteine and glycine-rich protein C
Mutational analysis and NMR spectroscopy of quail cysteine and glycine-rich protein CRP2 reveal an intrinsic segmental flexibility of LIM domains.
Related Articles Mutational analysis and NMR spectroscopy of quail cysteine and glycine-rich protein CRP2 reveal an intrinsic segmental flexibility of LIM domains.
J Mol Biol. 1999 Oct 1;292(4):893-908
Authors: Kloiber K, Weiskirchen R, Kräutler B, Bister K, Konrat R
The LIM domain is a conserved cysteine and histidine-containing structural module of two tandemly arranged zinc fingers. It has been...
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11-18-2010 08:31 PM
In-Cell NMR Spectroscopy
In-Cell NMR Spectroscopy
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 17 November 2010</br>
Andres Y., Maldonado , David S., Burz , Alexander, Shekhtman</br>
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11-18-2010 06:16 PM
[NMR paper] 13C NMR analysis of the cysteine-sulfenic acid redox center of enterococcal NADH pero
13C NMR analysis of the cysteine-sulfenic acid redox center of enterococcal NADH peroxidase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles 13C NMR analysis of the cysteine-sulfenic acid redox center of enterococcal NADH peroxidase.
Biochemistry. 1997 Jul 15;36(28):8611-8
Authors: Crane EJ, Vervoort J, Claiborne A
In order to characterize the native Cys42-sulfenic acid redox center of the flavoprotein NADH peroxidase by NMR, an expression protocol has been developed which yields the...
Detecting Intracellular Cysteine Redox States by in-Cell NMR Spectroscopy.
Linear Mode
