Related ArticlesVery fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.
J Am Chem Soc. 2005 Jun 8;127(22):8014-5
Authors: Schanda P, Brutscher B
We demonstrate for different protein samples that 2D 1H-15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle short-transient heteronuclear multiple quantum coherence experiment. This has enabled us to measure fast hydrogen-deuterium exchange rate constants along the backbone of a small globular protein fragment by real-time 2D NMR.
Monitoring Mechanistic Details in the Synthesis of Pyrimidines via Real-Time, Ultrafast Multidimensional NMR Spectroscopy
Monitoring Mechanistic Details in the Synthesis of Pyrimidines via Real-Time, Ultrafast Multidimensional NMR Spectroscopy
Zulay D. Pardo, Gregory L. Olsen, Mari?a Encarnacio?n Ferna?ndez-Valle, Lucio Frydman, Roberto Marti?nez-A?lvarez and Antonio Herrera
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja210154g/aop/images/medium/ja-2011-10154g_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja210154g
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/tEFGGh16-DU
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01-28-2012 05:27 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
Abstract It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate...
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01-27-2011 04:31 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
J Biomol NMR. 2011 Jan 21;
Authors: Etzkorn M, Böckmann A, Baldus M
It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all...
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01-22-2011 01:52 PM
[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] Combined frequency- and time-domain NMR spectroscopy. Application to fast protein res
Combined frequency- and time-domain NMR spectroscopy. Application to fast protein resonance assignment.
Related Articles Combined frequency- and time-domain NMR spectroscopy. Application to fast protein resonance assignment.
J Biomol NMR. 2004 May;29(1):57-64
Authors: Brutscher B
A simple and general method is presented to simplify multi-dimensional NMR spectra of isotope-labeled bio-molecules. The approach is based on band-selective Hadamard-type frequency encoding, which disperses the correlation peaks into different sub-spectra. This makes...
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11-24-2010 09:51 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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[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] Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labele
Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase.
Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9318-22
Authors: Hoeltzli SD, Frieden C
Escherichia coli dihydrofolate reductase (DHFR; EC 1.5.1.3) contains...