<sup>1</sup>H‐detektierte Festkörper‐NMR‐Studien wasserunzugänglicher Proteine in vitro und in situ

Medeiros‐Silva, João; Mance, Deni; Daniëls, Mark A.; Jekhmane, Shehrazade; Houben, Klaartje; Baldus, Marc; Weingarth, Markus

doi:10.1002/ange.201606594

Cited by 7 publications

(1 citation statement)

References 46 publications

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“…S2 and table S2), indicating that those regions are not exposed to water. The H/D exchange pattern for the SF is in agreement with previous observations for KcsA, where only Y78 and G79 (corresponding to Y66 and G67 in NaK2K) are water accessible (27,28), as well as with H/D exchange patterns deduced from MD simulations (fig. S3).…”

Section: Resultssupporting

confidence: 91%

The conduction pathway of potassium channels is water free under physiological conditions

et al. 2019

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Ion conduction through potassium channels is a fundamental process of life. On the basis of crystallographic data, it was originally proposed that potassium ions and water molecules are transported through the selectivity filter in an alternating arrangement, suggesting a “water-mediated” knock-on mechanism. Later on, this view was challenged by results from molecular dynamics simulations that revealed a “direct” knock-on mechanism where ions are in direct contact. Using solid-state nuclear magnetic resonance techniques tailored to characterize the interaction between water molecules and the ion channel, we show here that the selectivity filter of a potassium channel is free of water under physiological conditions. Our results are fully consistent with the direct knock-on mechanism of ion conduction but contradict the previously proposed water-mediated knock-on mechanism.

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Section: Resultssupporting

confidence: 91%

The conduction pathway of potassium channels is water free under physiological conditions

et al. 2019

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Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR

et al. 2017

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Obtaining unambiguous resonance assignments remains am ajor bottlenecki ns olid-state NMR studies of protein structure and dynamics.P articularly for supramolecular assemblies with large subunits (> 150 residues), the analysis of crowded spectral data presents ac hallenge,e ven if three-dimensional (3D) spectra are used. Here,w ep resent ap roton-detected 4D solid-state NMR assignment procedure that is tailored for large assemblies.T he key to recording 4D spectra with three indirect carbon or nitrogen dimensions with their inherently large chemical shift dispersion lies in the use of sparse non-uniform sampling (as lowa s2%). As ap roof of principle,weacquired 4D (H)COCANH, (H)CACONH, and (H)CBCANHs pectra of the 20 kDa bacteriophage tail-tube protein gp17.1 in at otal time of two and ah alf weeks.T hese spectra were sufficient to obtain complete resonance assignments in as traightforwardm anner without use of previous solution NMR data.

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Design Parameters of Tissue‐Engineering Scaffolds at the Atomic Scale

et al. 2019

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Stem‐cell behavior is regulated by the material properties of the surrounding extracellular matrix, which has important implications for the design of tissue‐engineering scaffolds. However, our understanding of the material properties of stem‐cell scaffolds is limited to nanoscopic‐to‐macroscopic length scales. Herein, a solid‐state NMR approach is presented that provides atomic‐scale information on complex stem‐cell substrates at near physiological conditions and at natural isotope abundance. Using self‐assembled peptidic scaffolds designed for nervous‐tissue regeneration, we show at atomic scale how scaffold‐assembly degree, mechanics, and homogeneity correlate with favorable stem cell behavior. Integration of solid‐state NMR data with molecular dynamics simulations reveals a highly ordered fibrillar structure as the most favorable stem‐cell scaffold. This could improve the design of tissue‐engineering scaffolds and other self‐assembled biomaterials.

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¹H‐detektierte Festkörper‐NMR‐Studien wasserunzugänglicher Proteine in vitro und in situ

Cited by 7 publications

References 46 publications

The conduction pathway of potassium channels is water free under physiological conditions

The conduction pathway of potassium channels is water free under physiological conditions

Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR

Design Parameters of Tissue‐Engineering Scaffolds at the Atomic Scale

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1H‐detektierte Festkörper‐NMR‐Studien wasserunzugänglicher Proteine in vitro und in situ

Cited by 7 publications

References 46 publications

The conduction pathway of potassium channels is water free under physiological conditions

The conduction pathway of potassium channels is water free under physiological conditions

Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR

Design Parameters of Tissue‐Engineering Scaffolds at the Atomic Scale

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Product

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¹H‐detektierte Festkörper‐NMR‐Studien wasserunzugänglicher Proteine in vitro und in situ