Andrea Bertarello
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View article: An Efficient and Stable Polarizing Agent for In-Cell Magic-Angle Spinning Dynamic Nuclear Polarization NMR Spectroscopy
An Efficient and Stable Polarizing Agent for In-Cell Magic-Angle Spinning Dynamic Nuclear Polarization NMR Spectroscopy Open
Nuclear Magnetic Resonance (NMR) spectroscopy would be a method of choice to follow biochemical events in cells because it can analyze molecules in complex environments. However, the intrinsically low sensitivity of NMR makes in-cell measu…
View article: Hierarchy of the Components in Spray-Dried, Protein-Excipient Particles Using DNP-Enhanced NMR Spectroscopy
Hierarchy of the Components in Spray-Dried, Protein-Excipient Particles Using DNP-Enhanced NMR Spectroscopy Open
Protein-based drugs are becoming increasingly important, but there are challenges associated with their formulation (for example, formulating stable inhalable aerosols while maintaining the proper long-term stability of the protein). Deter…
View article: <sup>1</sup>H Detected Relayed Dynamic Nuclear Polarization
<sup>1</sup>H Detected Relayed Dynamic Nuclear Polarization Open
Recently, it has been shown that methods based on the dynamics of 1H nuclear hyperpolarization in magic angle spinning (MAS) NMR experiments can be used to determine mesoscale structures in complex materials. However, these methods suffer …
View article: IN-CELL QUANTIFICATION OF DRUGS BY MAGIC ANGLE SPINNING DYNAMIC NUCLEAR POLARIZATION NMR
IN-CELL QUANTIFICATION OF DRUGS BY MAGIC ANGLE SPINNING DYNAMIC NUCLEAR POLARIZATION NMR Open
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View article: IN-CELL QUANTIFICATION OF DRUGS BY MAGIC ANGLE SPINNING DYNAMIC NUCLEAR POLARIZATION NMR
IN-CELL QUANTIFICATION OF DRUGS BY MAGIC ANGLE SPINNING DYNAMIC NUCLEAR POLARIZATION NMR Open
Raw data
View article: In-Cell Quantification of Drugs by Magic-Angle Spinning Dynamic Nuclear Polarization NMR
In-Cell Quantification of Drugs by Magic-Angle Spinning Dynamic Nuclear Polarization NMR Open
The determination of intracellular drug concentrations can provide a better understanding of the drug function and efficacy. Ideally, this should be performed nondestructively, with no modification of either the drug or the target, and wit…
View article: Author response: Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulation
Author response: Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulation Open
Article Figures and data Abstract Introduction Results Discussion Materials and methods Appendix 1 Data availability References Decision letter Author response Article and author information Metrics Abstract The CorA family of proteins reg…
View article: Mg <sup>2+</sup> -dependent conformational equilibria in CorA: an integrated view on transport regulation
Mg <sup>2+</sup> -dependent conformational equilibria in CorA: an integrated view on transport regulation Open
The CorA family of proteins regulates the homeostasis of divalent metal ions in many bacteria, archaea, and eukaryotic mitochondria, making it an important target in the investigation of the mechanisms of transport and its functional regul…
View article: Quantification of Magic Angle Spinning Dynamic Nuclear Polarization NMR Spectra
Quantification of Magic Angle Spinning Dynamic Nuclear Polarization NMR Spectra Open
NMR datasets of experiments used in the paper
View article: Quantification of Magic Angle Spinning Dynamic Nuclear Polarization NMR Spectra
Quantification of Magic Angle Spinning Dynamic Nuclear Polarization NMR Spectra Open
NMR datasets of experiments used in the paper
View article: Similarities and Differences among Protein Dynamics Studied by Variable Temperature Nuclear Magnetic Resonance Relaxation
Similarities and Differences among Protein Dynamics Studied by Variable Temperature Nuclear Magnetic Resonance Relaxation Open
Understanding and describing the dynamics of proteins is one of the major challenges in biology. Here, we use multifield variable-temperature NMR longitudinal relaxation (R-1) measurements to determine the hierarchical activation energies …
View article: Data forSimilarities and differences among protein dynamics studied by variable temperature NMR relaxation
Data forSimilarities and differences among protein dynamics studied by variable temperature NMR relaxation Open
Raw topspin data and matlab code for "Similarities and differences among protein dynamics studied by variable temperature NMR relaxation"
View article: Data forSimilarities and differences among protein dynamics studied by variable temperature NMR relaxation
Data forSimilarities and differences among protein dynamics studied by variable temperature NMR relaxation Open
Raw topspin data and matlab code for "Similarities and differences among protein dynamics studied by variable temperature NMR relaxation"
View article: Data forSimilarities and differences among protein dynamics studied by variable temperature NMR relaxation
Data forSimilarities and differences among protein dynamics studied by variable temperature NMR relaxation Open
Raw topspin data and matlab code for "Similarities and differences among protein dynamics studied by variable temperature NMR relaxation"
View article: Dynamic Nuclear Polarization Enhancement of 200 at 21.15 T Enabled by 65 kHz Magic Angle Spinning
Dynamic Nuclear Polarization Enhancement of 200 at 21.15 T Enabled by 65 kHz Magic Angle Spinning Open
Solid-state nuclear magnetic resonance under magic angle spinning (MAS) enhanced with dynamic nuclear polarization (DNP) is a powerful approach to characterize many important classes of materials, allowing access to previously inaccessible…
View article: Pico-meter resolution structure of the coordination sphere in the metal-binding site in a metalloprotein by NMR
Pico-meter resolution structure of the coordination sphere in the metal-binding site in a metalloprotein by NMR Open
NMR datasets and pulse sequences used in the paper
View article: Pico-meter resolution structure of the coordination sphere in the metal-binding site in a metalloprotein by NMR
Pico-meter resolution structure of the coordination sphere in the metal-binding site in a metalloprotein by NMR Open
NMR datasets and pulse sequences used in the paper
View article: Picometer Resolution Structure of the Coordination Sphere in the Metal-Binding Site in a Metalloprotein by NMR
Picometer Resolution Structure of the Coordination Sphere in the Metal-Binding Site in a Metalloprotein by NMR Open
Most of our understanding of chemistry derives from atomic-level structures obtained with single-crystal X-ray diffraction. Metal centers in X-ray structures of small organometallic or coordination complexes are often extremely well-define…
View article: RMN en rotation à l’angle magique de métalloprotéines paramagnétiques
RMN en rotation à l’angle magique de métalloprotéines paramagnétiques Open
Most of our understanding of metalloproteins derives from atomic or molecular structures obtained from diffraction methods on single crystal samples. However, not all proteins are amenable for diffraction studies, and even when a highly-re…
View article: Paramagnetic Properties of a Crystalline Iron–Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy
Paramagnetic Properties of a Crystalline Iron–Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy Open
We present the first solid-state NMR study of an iron-sulfur protein. The combined use of very fast (60 kHz) magic-angle spinning and tailored radiofrequency irradiation schemes allows the detection and the assignment of most of the 1H and…
View article: Frontispiece: NMR Spectroscopic Assignment of Backbone and Side‐Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils
Frontispiece: NMR Spectroscopic Assignment of Backbone and Side‐Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils Open
Protein Structures G. Pintacuda et al. show in their Communication on page 15504 ff. that with 111 kHz magic-angle spinning probes, high-resolution 1H-detected solid-state NMR spectra of proteins can be acquired without deuteration.
View article: Structure of fully protonated proteins by proton-detected magic-angle spinning NMR
Structure of fully protonated proteins by proton-detected magic-angle spinning NMR Open
Significance Protein structure determination is key to the detailed description of many biological processes. The critical factor that would allow general application of magic-angle spinning (MAS) solid-state NMR to this end is improvement…
View article: Structure of Fully Protonated Proteins by Proton-Detected Magic-Angle Spinning NMR
Structure of Fully Protonated Proteins by Proton-Detected Magic-Angle Spinning NMR Open
Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has focused on highly deuterated samples, in which only a small number of protons are introduced and observation of signals from side chains is extremely lim…