[NMR paper] A novel microfluidic rapid freeze-quench device for trapping reactions intermediates for high field EPR analysis
A novel microfluidic rapid freeze-quench device for trapping reactions intermediates for high field EPR analysis
Available online 5 March 2013
Publication year: 2013
Source:Journal of Magnetic Resonance</br>
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Rapid freeze quench electron paramagnetic resonance (RFQ)-EPR is a method for trapping short lived intermediates in chemical reactions and subjecting them to EPR spectroscopy investigation for their characterization. Two (or more) reacting components are mixed at room temperature and after some delay the mixture is sprayed into a cold trap and transferred into...
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NMR as a tool to identify and characterize protein folding intermediates
NMR as a tool to identify and characterize protein folding intermediates
Available online 12 September 2012
Publication year: 2012
Source:Archives of Biochemistry and Biophysics</br>
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NMR spectroscopy is one of the few biophysical methods that can provide atomic-level insight into the conformation of partially folded states and/or intermediates present along the protein folding pathway. Such studies are important not only within the context of the protein folding problem, but also to push forward the technique, due to the challenging nature of the systems studied....
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[NMR paper] Rapid amide proton exchange rates in peptides and proteins measured by solvent quench
Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.
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 Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.
Protein Sci. 1995 Apr;4(4):804-14
Authors: Zhang YZ,...
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[NMR paper] NMR and protein folding: equilibrium and stopped-flow studies.
NMR and protein folding: equilibrium and stopped-flow studies.
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 NMR and protein folding: equilibrium and stopped-flow studies.
Protein Sci. 1993 Dec;2(12):2007-14
Authors: Frieden C, Hoeltzli SD, Ropson IJ
NMR studies are now unraveling the structure of intermediates...