NMR spectroscopy is a powerful tool for research on protein dynamics. In the past decade, there has been significant progress in the development of NMR methods for studying charged side chains. In particular, NMR methods for lysine side-chain NH3+ groups
Dan Nguyen +3 more
doaj +1 more source
NMR Relaxation (NMRR) is an extremely useful quantitative technique for material science, particularly for studying polymers and porous materials. NMR Cryoporometry (NMRC) is a powerful technique for the measurement of pore-size distributions and total ...
J. Beau W. Webber
doaj +1 more source
Transient oligomers formed by intrinsically disordered proteins may be ‘invisible’ to direct detection yet remain accessible to solution NMR through equilibrium‐exchange measurements and pressure‐jump experiments. Complementary methods report on mass, stoichiometry, selected distance distributions, morphology, and internal packing.
Martin D. Gelenter, Ad Bax
wiley +1 more source
NMR RELAXATION METHODS TO DETECT PROTEIN DYNAMICS: EVALUATION OF ACCURACY, IMPROVEMENT OF THE METHODOLOGY, AND ITS APPLICATION [PDF]
Proteins are dynamic molecules whose ability to undergo conformational changes and fluctuations can impact their biological function, such as enzyme catalysis and substrate recognition. Mutations or perturbations that do not significantly change protein
Myint, Wazo
core
13C-direct detected NMR experiments for the sequential J-based resonance assignment of RNA oligonucleotides [PDF]
We present here a set of 13C-direct detected NMR experiments to facilitate the resonance assignment of RNA oligonucleotides. Three experiments have been developed: (1) the (H)CC-TOCSY-experiment utilizing a virtual decoupling scheme to assign the ...
Helena Kovacs +13 more
core +1 more source
Temperature dependence of 7Li NMR relaxation rates in Li3InCl6, Li3YCl6, Li1.48Al0.48Ge1.52(PO4)3 and LiPS5Cl [PDF]
Inorganic solid-state battery electrolytes show high ionic conductivities and enable the fabrication of all solid-state batteries. In this work, we present the temperature dependence of spin-lattice relaxation time (T1), spin-spin relaxation time (T2 ...
Carlos, Juarez-Yescas +4 more
core +1 more source
Adenosine triphosphate as a modulator of protein interactions and stability
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley +1 more source
Block Copolymer Micelles with an Intermediate Star-/Flower-Like Structure Studied by H-1 NMR Relaxometry [PDF]
H-1 NMR relaxation is used to study the self-assembly of a double thermoresponsive diblock copolymer in dilute aqueous solution. Above the first transition temperature, at which aggregation into micellar structures is observed, the trimethylsilyl (TMS ...
Boelens, Rolf +6 more
core +1 more source
Enhancing Low‐Temperature Performance of Sodium‐Ion Batteries via Anion‐Solvent Interactions
DOL is introduced into electrolytes as a co‐solvent, increasing slat solubility, ion conductivity, and the de‐solvent process, and forming an anion‐rich solvent shell due to its high interaction with anion. With the above virtues, the batteries using this electrolyte exhibit excellent cycling stability at low temperatures. Abstract Sodium‐ion batteries
Cheng Zheng +7 more
wiley +1 more source
Clathrate formation and dissociation in vapor/water/ice/hydrate systems in SBA-15, sol-gel and CPG porous media, as probed by NMR relaxation, novel protocol NMR cryoporometry, neutron scattering and ab initio quantum-mechanical molecular dynamics simulation [PDF]
The Gibbs-Thomson effect modifies the pressure and temperature at which clathrates occur, hence altering the depth at which they occur in the seabed. Nuclear magnetic resonance (NMR) measurements as a function of temperature are being conducted for water/
Webber, J. Beau W. +6 more
core +1 more source

