Among structural biology techniques, NMR spectroscopy offers unique capabilities that enable the atomic resolution studies of dynamic and heterogeneous biological systems under physiological and native conditions. Complex biological systems, however, often challenge NMR spectroscopists with their low sensitivity, crowded spectra or large linewidths that reflect their intricate interaction patterns and dynamics. While some of these challenges can be overcome with the development of new...
[NMR paper] (19)F NMR as a tool in chemical biology
(19)F NMR as a tool in chemical biology
We previously reviewed the use of ^(19)F NMR in the broad field of chemical biology and present here a summary of the literature from the last decade that has the technique as the central method of analysis. The topics covered include the synthesis of new fluorinated probes and their incorporation into macromolecules, the application of ^(19)F NMR to monitor protein-protein interactions, protein-ligand interactions,...
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02-24-2021 05:50 AM
[NMR paper] 19F NMR as a tool in chemical biology.
19F NMR as a tool in chemical biology.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.png Related Articles 19F NMR as a tool in chemical biology.
Beilstein J Org Chem. 2021;17:293-318
Authors: Gimenez D, Phelan A, Murphy CD, Cobb SL
Abstract
We previously reviewed the use of 19F NMR in the broad field of chemical biology and present here a summary of the literature from the last decade that has the technique as the central method of analysis. The...
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02-15-2021 01:33 PM
Basics of EPR for NMR spectroscopists
From The DNP-NMR Blog:
Basics of EPR for NMR spectroscopists
Dear NMR Enthusiast,
The 16th Global NMR Educational Tutorial will be given by Nino Wili, PhD student in Prof. Gunnar Jeschke's lab at ETH Zurich, Switzerland, on the topic:
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10-19-2020 05:07 PM
Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer
Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer
Abstract
Although Chemical Exchange Saturation Transfer (CEST) type NMR experiments have been used to study chemical exchange processes in molecules since the early 1960s, there has been renewed interest in the past several years in using this approach to study biomolecular conformational dynamics. The methodology is particularly powerful for the study of sparsely populated, transiently formed conformers that are recalcitrant to investigation using...
[NMR paper] Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.
Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.
Related Articles Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.
Prog Nucl Magn Reson Spectrosc. 2015 Apr;86-87C:41-64
Authors: Burmann BM, Hiller S
Abstract
The majority of proteins depend on a well-defined three-dimensional structure to obtain their functionality. In the cellular environment, the process of protein folding is guided by molecular chaperones to avoid misfolding, aggregation, and...
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04-29-2015 03:49 PM
[NMR paper] Protein production: feeding the crystallographers and NMR spectroscopists.
Protein production: feeding the crystallographers and NMR spectroscopists.
Related Articles Protein production: feeding the crystallographers and NMR spectroscopists.
Nat Struct Biol. 2000 Nov;7 Suppl:970-2
Authors: Edwards AM, Arrowsmith CH, Christendat D, Dharamsi A, Friesen JD, Greenblatt JF, Vedadi M
Protein purification efforts for structural genomics will focus on automation for the readily-expressed proteins, and process development for the more difficult ones, such as membrane proteins. Thousands of proteins are expected to be produced...
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11-19-2010 08:29 PM
The war of tools: how can NMR spectroscopists detect errors in their structures?
The war of tools: how can NMR spectroscopists detect errors in their structures?
Edoardo Saccenti and Antonio Rosato
Journal of Biomolecular NMR; 2008; 40(4) pp 251 - 261
Abstract:
Protein structure determination by NMR methods has started in the mid-eighties and has been growing steadily since then. Ca. 14% of the protein structures deposited in the PDB have been solved by NMR. The evaluation of the quality of NMR structures however is still lacking a well-established practice. In this work, we examined various tools for the assessment of structural quality to ascertain the extent to...