Sulfur-containing sites in proteins are of great importance for both protein structure and function, including enzymatic catalysis, signaling pathways, and recognition of ligands and protein partners. Selenium-77 is an NMR active spin-1/2 nucleus that shares many physiochemical properties with sulfur and can be readily introduced into proteins at sulfur sites without significant perturbations to the protein structure. The sulfur-containing amino acid methionine is commonly found at proteinâ??protein or proteinâ??ligand binding sites. Its selenium-containing counterpart, selenomethionine, has a broad chemical shift dispersion useful for NMR-based studies of complex systems. Methods such as (1H)-77Se-13C double cross polarization or {77Se}-13C REDOR could be valuable to map the local environment around selenium sites in proteins but have not been demonstrated to date. In this work, we explore these dipolar transfer mechanisms for structural characterization of the GB1 V39SeM variant of the model protein GB1 and demonstrate that 77Se-13C based correlations can be used to map the local environment around selenium sites in proteins. We have found that the general detection limit isâ??~â??5Â*Ã?, but longer range distances up toâ??~â??7Â*Ã? can be observed as well. This study establishes a framework for the future characterization of selenium sites at proteinâ??protein or proteinâ??ligand binding interfaces.
[NMR paper] Experimental Aspects of Polarization Optimized Experiments (POE) for Magic Angle Spinning Solid-State NMR of Microcrystalline and Membrane-Bound Proteins.
Experimental Aspects of Polarization Optimized Experiments (POE) for Magic Angle Spinning Solid-State NMR of Microcrystalline and Membrane-Bound Proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Experimental Aspects of Polarization Optimized Experiments (POE) for Magic Angle Spinning Solid-State NMR of Microcrystalline and Membrane-Bound Proteins.
Methods Mol Biol. 2018;1688:37-53
Authors: Gopinath T, Veglia G
Abstract
...
nmrlearner
Journal club
0
11-21-2017 10:10 PM
[NMR paper] Structure of Amorphous Selenium by 2D 77Se NMR Spectroscopy: An End to The Dilemma of Chain vs. Ring
Structure of Amorphous Selenium by 2D 77Se NMR Spectroscopy: An End to The Dilemma of Chain vs. Ring
Amorphous selenium, owing to its tremendous technological importance and perhaps to its chemical simplicity, has been studied for nearly a century and yet an unequivocal structural description of this material remains lacking in the literature to date. The primary controversy regarding the structure of a-Se relates to the relative fraction of Se atoms residing in infinite (Se) chains vs. in Se8 rings. Here we present the results of a two-dimensional solid-state 77Se nuclear magnetic...
nmrlearner
Journal club
0
06-26-2017 08:42 AM
Sequential backbone assignment based on dipolar amide-to-amide correlation experiments
Sequential backbone assignment based on dipolar amide-to-amide correlation experiments
Abstract
Proton detection in solid-state NMR has seen a tremendous increase in popularity in the last years. New experimental techniques allow to exploit protons as an additional source of information on structure, dynamics, and protein interactions with their surroundings. In addition, sensitivity is mostly improved and ambiguity in assignment experiments reduced. We show here that, in the solid state, sequential amide-to-amide correlations turn out to be an...
nmrlearner
Journal club
0
05-15-2015 07:52 AM
[NMR paper] Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins.
Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins.
Related Articles Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins.
J Magn Reson. 2014 Mar 4;242C:180-188
Authors: Chevelkov V, Habenstein B, Loquet A, Giller K, Becker S, Lange A
Abstract
Proton-detected solid-state NMR was applied to a highly deuterated insoluble, non-crystalline biological assembly, the Salmonella typhimurium type iii secretion system...
nmrlearner
Journal club
0
03-29-2014 01:00 PM
Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins
Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins
Publication date: Available online 4 March 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Veniamin Chevelkov , Birgit Habenstein , Antoine Loquet , Karin Giller , Stefan Becker , Adam Lange</br>
Proton-detected solid-state NMR was applied to a highly deuterated insoluble, non-crystalline biological assembly, the Salmonella typhimurium type iii secretion system (T3SS) needle. Spectra of very high resolution and sensitivity were obtained...
77Se-13C based dipolar correlation experiments to map selenium sites in microcrystalline proteins
Linear Mode
