Related ArticlesCorrection: Exploring exchange processes in proteins by paramagnetic perturbation of NMR spectra.
Phys Chem Chem Phys. 2020 Jul 16;:
Authors: Hunashal Y, Cantarutti C, Giorgetti S, Marchese L, Molinari H, Niccolai N, Fogolari F, Esposito G
Abstract
Correction for 'Exploring exchange processes in proteins by paramagnetic perturbation of NMR spectra' by Yamanappa Hunashal et al., Phys. Chem. Chem. Phys., 2020, 22, 6247-6259, DOI: 10.1039/c9cp06950j.
PMID: 32672261 [PubMed - as supplied by publisher]
[NMR paper] Exploring exchange processes in proteins by paramagnetic perturbation of NMR spectra.
Exploring exchange processes in proteins by paramagnetic perturbation of NMR spectra.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.rsc-cdn.org-oxygen-assets-logo-rsc-logo-btn-small.gif Related Articles Exploring 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...
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03-07-2020 06:20 PM
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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03-30-2017 06:42 PM
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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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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[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. 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
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Correction: Exploring exchange processes in proteins by paramagnetic perturbation of NMR spectra.
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