HETex-SOFAST NMR (Schanda et al. in J Biomol NMR 33:199â??211, 2006) has been proposed some years ago as a fast and sensitive method for semi-quantitative measurement of site-specific amide-water hydrogen exchange effects along the backbone of proteins. Here we extend this concept to BEST readout sequences that provide a better resolution at the expense of some loss in sensitivity. We discuss the theoretical background and implementation of the experiment, and demonstrate its performance for an intrinsically disordered protein, 2 well folded globular proteins, and a transiently populated folding intermediate state. We also provide a critical evaluation of the level of accuracy that can be obtained when extracting quantitative exchange rates from HETex NMR measurements.
[NMR paper] Measuring translational diffusion coefficients of peptides and proteins by PFG-NMR using band-selective RF pulses.
Measuring translational diffusion coefficients of peptides and proteins by PFG-NMR using band-selective RF pulses.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Measuring translational diffusion coefficients of peptides and proteins by PFG-NMR using band-selective RF pulses.
Eur Biophys J. 2014 May 14;
Authors: Yao S, Weber DK, Separovic F, Keizer DW
Abstract
Molecular translational self-diffusion, a measure of diffusive...
[NMR paper] Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Feb 28;
Authors: Vallurupalli P, Kay LE
Abstract
Seeing the invisible: A 13 CO NMR chemical exchange saturation transfer (CEST) experiment for the study of "invisible" excited protein states with lifetimes on the order of 5-50 ms has been developed. The 13 CO chemical...
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03-02-2013 11:45 AM
[NMR paper] Rapid Characterization of Hydrogen Exchange in Proteins.
Rapid Characterization of Hydrogen Exchange in Proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Rapid Characterization of Hydrogen Exchange in Proteins.
Angew Chem Int Ed Engl. 2013 Jan 22;
Authors: Thakur A, Chandra K, Dubey A, D'Silva P, Atreya HS
Abstract
Kinetics and thermodynamics of amide hydrogen exchange in proteins can be investigated with two-dimensional (13) CO-(15) N NMR correlation experiments. The spectra are...
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[NMR paper] Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Related Articles Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
J Biomol NMR. 2005 Jul;32(3):195-207
Authors: Böckmann A, Juy M, Bettler E, Emsley L, Galinier A, Penin F, Lesage A
We report site-resolved observation of hydrogen exchange in the micro-crystalline protein Crh. Our approach is based on the use of proton T2' -selective 1H-13C-13C correlation spectra for...
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[NMR paper] 3D NMR experiments for measuring 15N relaxation data of large proteins: application t
3D NMR experiments for measuring 15N relaxation data of large proteins: application to the 44 kDa ectodomain of SIV gp41.
Related Articles 3D NMR experiments for measuring 15N relaxation data of large proteins: application to the 44 kDa ectodomain of SIV gp41.
J Magn Reson. 1998 Dec;135(2):368-72
Authors: Caffrey M, Kaufman J, Stahl SJ, Wingfield PT, Gronenborn AM, Clore GM
A suite of 3D NMR experiments for measuring 15N-¿1H¿ NOE, 15N T1, and 15N T1rho values in large proteins, uniformly labeled with 15N and 13C, is presented. These...
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[NMR paper] Hydrogen exchange properties of proteins in native and denatured states monitored by
Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and 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 Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.
Protein Sci. 1997 Jun;6(6):1316-24
Authors: Chung EW,...
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08-22-2010 03:31 PM
[NMR paper] Hydrogen exchange properties of proteins in native and denatured states monitored by
Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and 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 Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.
Protein Sci. 1997 Jun;6(6):1316-24
Authors: Chung EW,...