Authors: Hu Y, Cheng K, He L, Zhang X, Jiang B, Jiang L, Li C, Wang G, Yang Y, Liu M
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is a well-established method for analyzing protein structure, interaction, and dynamics at atomic resolution and in various sample states including solution state, solid state, and membranous environment. Thanks to rapid NMR methodology development, the past decade has witnessed a growing number of protein NMR studies in complex systems ranging from membrane mimetics to living cells, which pushes the research frontier further toward physiological environments and offers unique insights in elucidating protein functional mechanisms. In particular, in-cell NMR has become a method of choice for bridging the huge gap between structural biology and cell biology. Herein, we review the recent developments and applications of NMR methods for protein analysis in close-to-physiological environments, with special emphasis on in-cell protein structural determination and the analysis of protein dynamics, both difficult to be accessed by traditional methods.
PMID: 33439619 [PubMed - as supplied by publisher]
[ASAP] Methyl-Based NMR Spectroscopy Methods for Uncovering Structural Dynamics in Large Proteins and Protein Complexes
Methyl-Based NMR Spectroscopy Methods for Uncovering Structural Dynamics in Large Proteins and Protein Complexes
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00953/20181026/images/medium/bi-2018-00953s_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00953
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11-25-2018 06:02 AM
Protein resonance assignment at MAS frequencies approaching 100Â*kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods
Protein resonance assignment at MAS frequencies approaching 100Â*kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods
Abstract
We discuss the optimum experimental conditions to obtain assignment spectra for solid proteins at magic-angle spinning (MAS) frequencies around 100Â*kHz. We present a systematic examination of the MAS dependence of the amide proton T 2â?² times and a site-specific comparison of T 2â?² at 93Â*kHz versus 60Â*kHz MAS frequency. A...
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08-13-2015 02:00 PM
[NMR images] Methods in Protein Structure and Stability Analysis: NMR and EPR ...
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8/04/2014 7:46:05 AM GMT
Methods in Protein Structure and Stability Analysis: NMR and EPR ...
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04-08-2014 07:45 AM
[NMR paper] NMR-based analysis of protein-ligand interactions.
NMR-based analysis of protein-ligand interactions.
NMR-based analysis of protein-ligand interactions.
Anal Bioanal Chem. 2013 Apr 18;
Authors: Cala O, Guillière F, Krimm I
Abstract
Physiological processes are mainly controlled by intermolecular recognition mechanisms involving protein-protein and protein-ligand (low molecular weight molecules) interactions. One of the most important tools for probing these interactions is high-field solution nuclear magnetic resonance (NMR) through protein-observed and ligand-observed experiments, where...
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04-18-2013 10:12 PM
[NMR paper] NMR-based methods and strategies for drug discovery.
NMR-based methods and strategies for drug discovery.
Related Articles NMR-based methods and strategies for drug discovery.
Chem Soc Rev. 2003 Nov;32(6):365-72
Authors: Salvatella X, Giralt E
Nuclear Magnetic Resonance (NMR) spectroscopy has long been a favourite tool of chemists interested in host-guest systems because it permits access to a wealth of information about the molecular recognition reaction. NMR has evolved dramatically in the last 15 years and, in parallel with the development of NMR methods for the determination of protein...
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11-24-2010 09:16 PM
[NMR paper] Automated analysis of protein NMR assignments using methods from artificial intellige
Automated analysis of protein NMR assignments using methods from artificial intelligence.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Automated analysis of protein NMR assignments using methods from artificial intelligence.
J Mol Biol. 1997 Jun 20;269(4):592-610
Authors: Zimmerman DE, Kulikowski CA, Huang Y, Feng W, Tashiro M, Shimotakahara S, Chien C, Powers R, Montelione GT
An expert system for determining resonance assignments from NMR spectra of proteins is...
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08-22-2010 03:31 PM
[NMR paper] Automated analysis of protein NMR assignments using methods from artificial intellige
Automated analysis of protein NMR assignments using methods from artificial intelligence.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Automated analysis of protein NMR assignments using methods from artificial intelligence.
J Mol Biol. 1997 Jun 20;269(4):592-610
Authors: Zimmerman DE, Kulikowski CA, Huang Y, Feng W, Tashiro M, Shimotakahara S, Chien C, Powers R, Montelione GT
An expert system for determining resonance assignments from NMR spectra of proteins is...
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08-22-2010 03:03 PM
Structure-oriented methods for protein NMR data analysis
Structure-oriented methods for protein NMR data analysis
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 3 March 2010</br>
Guillermo A., Bermejo , Miguel, Llinás</br>
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