Related ArticlesExploring exchange processes in proteins by paramagnetic perturbation of NMR spectra.
Phys Chem Chem Phys. 2020 Mar 04;:
Authors: Hunashal Y, Cantarutti C, Giorgetti S, Marchese L, Molinari H, Niccolai N, Fogolari F, Esposito G
Abstract
The effect of extrinsic paramagnetic probes on NMR relaxation rates for surface mapping of proteins and other biopolymers is a widely investigated and powerful NMR technique. Here we describe a new application of those probes. It relies on the setting of the relaxation delay to generate magnetization equilibrium and off-equilibrium conditions, in order to tailor the extent of steady state signal recovery with and without the water-soluble nitroxide Tempol. With this approach it is possible to identify signals whose relaxation is affected by exchange processes and, from the relative assignments, to map the protein residues involved in association or conformational interconversion processes on a micro-to-millisecond time scale. This finding is confirmed by the comparison with the results obtained from relaxation dispersion measurements. This simple and convenient method allows preliminary inspection to highlight regions where structural or chemical exchange events are operative, in order to focus on quantitative subsequent determinations by transverse relaxation dispersion experiments or analogous NMR relaxation studies, and/or to gain insights into the predictions of calculations.
PMID: 32129386 [PubMed - as supplied by publisher]
Longitudinal relaxation optimized amide 1 H-CEST experiments for studying slow chemical exchange processes in fully protonated proteins
Longitudinal relaxation optimized amide 1 H-CEST experiments for studying slow chemical exchange processes in fully protonated proteins
Abstract
Chemical Exchange Saturation Transfer (CEST) experiments are increasingly used to study slow timescale exchange processes in biomolecules. Although 15N- and 13C-CEST have been the approaches of choice, the development of spin state selective 1H-CEST pulse sequences that separate the effects of chemical and dipolar exchange significantly increases the utility of 1H-based experiments. Pulse schemes have been...
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Exploring Folding Cooperativity of a Repeat Protein Folding by 2D-NMR Detected Pressure Perturbation
Exploring Folding Cooperativity of a Repeat Protein Folding by 2D-NMR Detected Pressure Perturbation
Publication date: 16 February 2016
Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br>
Author(s): Martin J. Fossat, Angel Garcia, Doug Barrick, Christian Roumestand, Catherine A. Royer</br>
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02-17-2016 07:50 PM
Site-Resolved Measurementof Microsecond-to-MillisecondConformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy
Site-Resolved Measurementof Microsecond-to-MillisecondConformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy
Martin Tollinger, Astrid C. Sivertsen, Beat H. Meier, Matthias Ernst and Paul Schanda
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja303591y/aop/images/medium/ja-2012-03591y_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja303591y
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http://feeds.feedburner.com/~r/acs/jacsat/~4/ZVmFwVkbuRs
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08-29-2012 04:28 AM
Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.
Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.
Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.
Protein Sci. 2011 Feb;20(2):229-46
Authors: Clore GM
Sparsely populated states of macromolecules, characterized by short lifetimes and high free-energies relative to the predominant ground state, often play a key role in many biological, chemical, and biophysical processes. In this review, we briefly summarize various new developments in NMR...
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06-04-2011 11:26 AM
[NMR paper] Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid s
Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid state NMR spectroscopy.
Related Articles Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid state NMR spectroscopy.
J Mol Biol. 2002 Nov 8;323(5):899-907
Authors: Stumber M, Geyer M, Graf R, Kalbitzer HR, Scheffzek K, Haeberlen U
The folding, structure and biological function of many proteins are inherently dynamic properties of the protein molecule. Often, the respective molecular processes are preserved upon protein...
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11-24-2010 08:58 PM
[NMR paper] Probing protein structure by solvent perturbation of NMR spectra. Photochemically ind
Probing protein structure by solvent perturbation of NMR spectra. Photochemically induced dynamic nuclear polarization and paramagnetic perturbation techniques applied to the study of the molten globule state of alpha-lactalbumin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Probing protein structure by solvent perturbation of NMR spectra. Photochemically induced dynamic nuclear polarization and paramagnetic perturbation techniques applied to the study of the...
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[NMR paper] Probing protein structure by solvent perturbation of NMR spectra. A comparison with p
Probing protein structure by solvent perturbation of NMR spectra. A comparison with photochemically induced dynamic nuclear polarization techniques applied to native alpha-lactalbumin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Probing protein structure by solvent perturbation of NMR spectra. A comparison with photochemically induced dynamic nuclear polarization techniques applied to native alpha-lactalbumin.
Eur J Biochem. 1995 Jan 15;227(1-2):78-86...
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[NMR paper] Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A s
Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A study of bovine serum albumin by diverse NMR techniques.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A study of bovine serum albumin by diverse NMR techniques.
Biophys J. 1990 Nov;58(5):1183-97
Authors: Kimmich R, Gneiting T, Kotitschke K, Schnur G
Experimental frequency, concentration, and...