The NMR spectra of side-chain protons in proteins provide important information, not only about their structure and dynamics, but also about the mechanisms that regulate interactions between macromolecules. However, in the solid-state, these resonances are particularly difficult to resolve, even in relatively small proteins. We show that magic-angle-spinning (MAS) frequencies of 160 kHz, combined with a high magnetic field of 1200 MHz proton Larmor frequency, significantly improve their spectral...
[NMR paper] 1H, 15N and 13C backbone and side chain solution NMR assignments of the TPM domain-containing protein of the thermophilic bacterium Rhodothermus marinus
1H, 15N and 13C backbone and side chain solution NMR assignments of the TPM domain-containing protein of the thermophilic bacterium Rhodothermus marinus
The InterPro family IPR007621 TPM_phosphatase is a widely conserved family of protein domains found in prokaryotes, plants and invertebrates. Despite similar predicted protein folding, members of this family are involved in different cellular processes. In recent years, the structural and biochemical characterization of evolutionarily divergent TPM domains has shown their ability to hydrolyze phosphate groups of different substrates....
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08-06-2023 03:39 PM
Proton TOCSY NMR relaxation rates quantitate protein side chain mobility in the Pin1 WW domain
Proton TOCSY NMR relaxation rates quantitate protein side chain mobility in the Pin1 WW domain
Abstract
Protein side chain dynamics play a vital role in many biological processes, but differentiating mobile from rigid side chains remains a technical challenge in structural biology. Solution NMR spectroscopy is ideally suited for this but suffers from limited signal-to-noise, signal overlap, and a need for fractional 13C or 2H labeling. Here we introduce a simple strategy measuring initial 1H relaxation rates during a 1H TOCSY sequence like DIPSI-2,...
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07-22-2022 11:46 PM
[NMR paper] Proton TOCSY NMR relaxation rates quantitate protein side chain mobility in the Pin1 WW domain
Proton TOCSY NMR relaxation rates quantitate protein side chain mobility in the Pin1 WW domain
Protein side chain dynamics play a vital role in many biological processes, but differentiating mobile from rigid side chains remains a technical challenge in structural biology. Solution NMR spectroscopy is ideally suited for this but suffers from limited signal-to-noise, signal overlap, and a need for fractional ^(13)C or ²H labeling. Here we introduce a simple strategy measuring initial ¹H relaxation rates during a ¹H TOCSY sequence like DIPSI-2, which can be appended to the beginning of...
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07-22-2022 11:46 PM
[NMR paper] Unambiguous Side-Chain Assignments for Solid-State NMR Structure Elucidation of Nondeuterated Proteins via a Combined 5D/4D Side-Chain-to-Backbone Experiment
Unambiguous Side-Chain Assignments for Solid-State NMR Structure Elucidation of Nondeuterated Proteins via a Combined 5D/4D Side-Chain-to-Backbone Experiment
Owing to fast-magic-angle-spinning technology, proton-detected solid-state NMR has been facilitating the analysis of insoluble, crystalline, sedimented, and membrane proteins. However, potential applications have been largely restricted by limited access to side-chain resonances. The recent availability of spinning frequencies exceeding 100 kHz in principle now allows direct probing of all protons without the need for partial...
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02-17-2022 11:34 AM
[NMR paper] Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments
Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments
Nuclear magnetic resonance (NMR) is a mainstay of biophysical studies that provides atomic level readouts to formulate molecular mechanisms. Side chains are particularly important to derive mechanisms involving proteins as they carry functional groups, but NMR studies of side chains are often limited by challenges in assigning their signals. Here, we designed a novel computational method that combines spectral derivatives and matrix square-rooting to produce reliable 4D covariance maps from...
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09-14-2021 12:38 AM
[NMR paper] Protein Side-Chain-DNA Contacts Probed by Fast Magic-Angle Spinning NMR.
Protein Side-Chain-DNA Contacts Probed by Fast Magic-Angle Spinning NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Protein Side-Chain-DNA Contacts Probed by Fast Magic-Angle Spinning NMR.
J Phys Chem B. 2020 Nov 25;:
Authors: Lacabanne D, Boudet J, Malär AA, Wu P, Cadalbert R, Salmon L, Allain FH, Meier BH, Wiegand T
Abstract
Protein-nucleic acid interactions are essential in a variety of biological events ranging from the replication of genomic...
[NMR paper] Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelle
Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles.
Related Articles Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles.
J Biomol NMR. 2002 Aug;23(4):289-301
Authors: Hilty C, Fernández C, Wider G, Wüthrich K
Sequence-specific assignments have been obtained for side chain methyl resonances of Val, Leu and Ile in the outer membrane protein X (OmpX) from Escherichia coli reconstituted in 60 kDa micelles in aqueous solution. Using previously established techniques, OmpX was...
High and fast: NMR protein-proton side-chain assignments at 160 kHz and 1.2 GHz
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