[NMR paper] Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR Spectroscopy
Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR Spectroscopy
Intrinsically disordered proteins are abundant in eukaryotic systems, but they remain largely elusive pharmacological targets. NMR spectroscopy proved to be a suitable method to study these proteins and their interaction with one another or with drug candidates. Although NMR can give atomistic information about these interplays, molecular complexity due to severe spectral overlap, limited sample stability, and quantity remain an issue and hamper widespread...
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[NMR paper] Isotope labeling for studying RNA by solid-state NMR spectroscopy.
Isotope labeling for studying RNA by solid-state NMR spectroscopy.
Related Articles Isotope labeling for studying RNA by solid-state NMR spectroscopy.
J Biomol NMR. 2018 Apr 12;:
Authors: Marchanka A, Kreutz C, Carlomagno T
Abstract
Nucleic acids play key roles in most biological processes, either in isolation or in complex with proteins. Often they are difficult targets for structural studies, due to their dynamic behavior and high molecular weight. Solid-state nuclear magnetic resonance spectroscopy (ssNMR) provides a unique...
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04-14-2018 01:49 PM
Isotope labeling for studying RNA by solid-state NMR spectroscopy
Isotope labeling for studying RNA by solid-state NMR spectroscopy
Abstract
Nucleic acids play key roles in most biological processes, either in isolation or in complex with proteins. Often they are difficult targets for structural studies, due to their dynamic behavior and high molecular weight. Solid-state nuclear magnetic resonance spectroscopy (ssNMR) provides a unique opportunity to study large biomolecules in a non-crystalline state at atomic resolution. Application of ssNMR to RNA, however, is still at an early stage of development and presents...
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04-12-2018 01:11 PM
[NMR paper] Domain interactions of C-terminal Src Kinase determined through NMR spectroscopy with segmental isotope labeling.
Domain interactions of C-terminal Src Kinase determined through NMR spectroscopy with segmental isotope labeling.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Domain interactions of C-terminal Src Kinase determined through NMR spectroscopy with segmental isotope labeling.
Protein Cell. 2017 01;8(1):67-71
Authors: Liu...
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01-10-2018 12:35 AM
[NMR paper] Multiple acquisition of magic angle spinning solid-state NMR experiments using one receiver: Application to microcrystalline and membrane protein preparations.
Multiple acquisition of magic angle spinning solid-state NMR experiments using one receiver: Application to microcrystalline and membrane protein preparations.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Multiple acquisition of magic angle spinning solid-state NMR experiments using one receiver: Application to microcrystalline and membrane protein preparations.
J Magn Reson. 2015 Apr;253:143-53
Authors: Gopinath T, Veglia G
Abstract
Solid-state NMR...
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03-24-2015 09:58 PM
Multiple acquisition of magic angle spinning solid-state NMR experiments using one receiver: Application to microcrystalline and membrane protein preparations
Multiple acquisition of magic angle spinning solid-state NMR experiments using one receiver: Application to microcrystalline and membrane protein preparations
Publication date: April 2015
Source:Journal of Magnetic Resonance, Volume 253</br>
Author(s): T. Gopinath , Gianluigi Veglia</br>
Solid-state NMR spectroscopy of proteins is a notoriously low-throughput technique. Relatively low-sensitivity and poor resolution of protein samples require long acquisition times for multidimensional NMR experiments. To speed up data acquisition, we developed a family of...
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03-20-2015 01:48 AM
[NMR paper] Isotope labeling strategies for analysis of an ion channel cytoplasmic domain by NMR spectroscopy.
Isotope labeling strategies for analysis of an ion channel cytoplasmic domain by NMR spectroscopy.
Related Articles Isotope labeling strategies for analysis of an ion channel cytoplasmic domain by NMR spectroscopy.
Methods Mol Biol. 2013;998:289-300
Authors: Abarca-Heidemann K, Duchardt-Ferner E, Woehnert J, Rothberg BS
Abstract
As large, multimeric, integral membrane proteins, ion channels pose technical challenges to analysis by NMR spectroscopy. Here we present a strategy to overcome some of these technical hurdles, using a...
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03-27-2013 03:33 PM
[NMR paper] New developments in isotope labeling strategies for protein solution NMR spectroscopy
New developments in isotope labeling strategies for protein solution NMR spectroscopy.
Related Articles New developments in isotope labeling strategies for protein solution NMR spectroscopy.
Curr Opin Struct Biol. 2000 Oct;10(5):585-92
Authors: Goto NK, Kay LE
The development of novel isotope labeling strategies for proteins has facilitated the study of the structure and dynamics of these molecules. In addition, the recent emergence of alternative methods of bacterial expression for obtaining isotopically labeled proteins permits the study of...
Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR Spectroscopy - ACS Publications
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