* In the context of a project funded by European Research Council, two postdoctoral positions are available at the Structural Biology Institute in Grenoble (France) to study by real-time NMR the Folding & Mechanisms of Protein Quality Control (PQC) Machineries. Selected candidates will use latest NMR technologies developed at IBS to characterize self-assembly and functionally important structural rearrangements of large PQC machineries isolated at IBS.
Real-Time NMR Studies of Electrochemical Double-Layer Capacitors
Real-Time NMR Studies of Electrochemical Double-Layer Capacitors
Hao Wang, Thomas K.-J. Ko?ster, Nicole M. Trease, Julie Se?galini, Pierre-Louis Taberna, Patrice Simon, Yury Gogotsi and Clare P. Grey
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2072115/aop/images/medium/ja-2011-072115_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2072115
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/-UeWTD49pVw
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11-12-2011 01:40 AM
[NMR paper] Protein folding studied by real-time NMR spectroscopy.
Protein folding studied by real-time NMR spectroscopy.
Related Articles Protein folding studied by real-time NMR spectroscopy.
Methods. 2004 Sep;34(1):65-74
Authors: Zeeb M, Balbach J
Real-time NMR spectroscopy developed to a generally applicable method to follow protein folding reactions. It combines the access to high resolution data with kinetic experiments allowing very detailed insights into the development of the protein structure during different steps of folding. The present review concentrates mainly on the progress of real-time NMR...
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11-24-2010 10:01 PM
[NMR paper] Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Related Articles Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
J Mol Biol. 2003 May 16;328(5):1161-71
Authors: Mizuguchi M, Kroon GJ, Wright PE, Dyson HJ
At low ionic strength, apoplastocyanin forms an unfolded state under non-denaturing conditions. The refolding of this state is sufficiently slow to allow real-time NMR experiments to be performed. Folding of apoplastocyanin, initiated by the addition of salt and followed by real-time 2D 1H-15N...
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11-24-2010 09:01 PM
[NMR paper] Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optic
Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy.
Related Articles Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy.
J Mol Biol. 1998 Feb 27;276(3):657-67
Authors: Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM
The refolding kinetics of the chemically denatured SH3 domain of phosphatidylinositol 3'-kinase (PI3-SH3) have been monitored by real-time one-dimensional 1H NMR coupled with a variety of other biophysical techniques. These...
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11-17-2010 11:06 PM
[NMR paper] Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
Related Articles Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
FEBS Lett. 1998 Feb 13;423(1):110-2
Authors: Killick TR, Freund SM, Fersht AR
The folding and unfolding of proteins is generally assumed to be so co-operative that the overall process may be followed by a single probe, such as tryptophan fluorescence. Folding kinetics of three mutants of barnase and chymotrypsin inhibitor 2 (CI2) were studied by real-time NMR....
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[NMR paper] Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolat
Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy.
Biochemistry. 1996 Dec 24;35(51):16843-51
Authors: Hoeltzli SD, Frieden C
Escherichia coli dihydrofolate reductase (ecDHFR, EC1.5.1.3) contains 5 tryptophan residues that have...
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08-22-2010 02:20 PM
[NMR paper] Following protein folding in real time using NMR spectroscopy.
Following protein folding in real time using NMR spectroscopy.
Related Articles Following protein folding in real time using NMR spectroscopy.
Nat Struct Biol. 1995 Oct;2(10):865-70
Authors: Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM
The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative...
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08-22-2010 03:50 AM
[NMR paper] Real-time NMR studies on a transient folding intermediate of barstar.
Real-time NMR studies on a transient folding intermediate of barstar.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Real-time NMR studies on a transient folding intermediate of barstar.
Protein Sci. 1999 Jun;8(6):1286-91
Authors: Killick TR, Freund SM, Fersht AR
The refolding of barstar, the intracellular...
Real-time NMR Studies of the Folding & Mechanisms of Protein Quality Control Machiner
Linear Mode
