Solid-state NMR has great potential for investigating molecular structure, dynamics, and organization of the stratum corneum, the outer 10-20 ?m of the skin, but is hampered by the unfeasibility of isotope labelling as generally required to reach sufficient signal-to-noise ratio for the more informative multidimensional NMR techniques. In this preliminary study of pig stratum corneum at 35 °C and water-free conditions, we demonstrate that cryogenic probe technology offers sufficient signal boost...
Amino-acid selective isotope labeling enables simultaneous overlapping signal decomposition and information extraction from NMR spectra
Amino-acid selective isotope labeling enables simultaneous overlapping signal decomposition and information extraction from NMR spectra
Abstract
Signal overlapping is a major bottleneck for protein NMR analysis. We propose a new method, stable-isotope-assisted parameter extraction (SiPex), to resolve overlapping signals by a combination of amino-acid selective isotope labeling (AASIL) and tensor decomposition. The basic idea of Sipex is that overlapping signals can be decomposed with the help of intensity patterns derived from quantitative fractional...
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02-29-2020 09:52 PM
[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...
[NMR paper] Isotope Labeling of Eukaryotic Membrane Proteins in Yeast for Solid-State NMR.
Isotope Labeling of Eukaryotic Membrane Proteins in Yeast for Solid-State NMR.
Related Articles Isotope Labeling of Eukaryotic Membrane Proteins in Yeast for Solid-State NMR.
Methods Enzymol. 2015;565:193-212
Authors: Fan Y, Emami S, Munro R, Ladizhansky V, Brown LS
Abstract
Solid-state NMR (ssNMR) is a rapidly developing technique for exploring structure and dynamics of membrane proteins, but its progress is hampered by its low sensitivity. Despite the latest technological advances, routine ssNMR experiments still require...
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11-19-2015 05:22 PM
[NMR paper] Unambiguous Assignment of Short- and Long-Range Structural Restraints by Solid-State NMR Spectroscopy with Segmental Isotope Labeling.
Unambiguous Assignment of Short- and Long-Range Structural Restraints by Solid-State NMR Spectroscopy with Segmental Isotope Labeling.
Related Articles Unambiguous Assignment of Short- and Long-Range Structural Restraints by Solid-State NMR Spectroscopy with Segmental Isotope Labeling.
Chembiochem. 2014 Nov 12;
Authors: Schubeis T, Lührs T, Ritter C
Abstract
We present an efficient method for the reduction of spectral complexity in the solid-state NMR spectra of insoluble protein assemblies, without loss of signal intensity....
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11-14-2014 08:40 PM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Abstract Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties with achieving proper folding, membrane insertion, and native-like post-translational modifications frequently disqualify bacterial expression systems. On the other hand, eukaryotic cell cultures can be prohibitively expensive. One of the viable alternatives,...
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Proteins
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01-22-2011 03:46 AM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
J Biomol NMR. 2011 Jan 19;
Authors: Fan Y, Shi L, Ladizhansky V, Brown LS
Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties...