scholarly journals Spatial Distribution of Silica-Bound Catalytic Organic Functional Groups Can Now Be Revealed by Conventional and DNP-Enhanced Solid-State NMR Methods

ACS Catalysis ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 7238-7249 ◽  
Author(s):  
Takeshi Kobayashi ◽  
Marek Pruski
Keyword(s):  
Spatial Distribution ◽  
Solid State ◽  
Functional Groups ◽  
Solid State Nmr ◽  
Organic Functional Groups ◽  
Nmr Methods

scholarly journals Spatial distribution of organic functional groups supported on mesoporous silica nanoparticles: a study by conventional and DNP-enhanced 29Si solid-state NMR

2017 ◽  
Vol 19 (3) ◽  
pp. 1781-1789 ◽  
Author(s):  
Takeshi Kobayashi ◽  
Dilini Singappuli-Arachchige ◽  
Zhuoran Wang ◽  
Igor I. Slowing ◽  
Marek Pruski
Keyword(s):  
Spatial Distribution ◽  
Solid State ◽  
Mesoporous Silica ◽  
Silica Nanoparticles ◽  
Functional Groups ◽  
Solid State Nmr ◽  
Mesoporous Silica Nanoparticles ◽  
Spatial Distributions ◽  
Organic Functional Groups

DNP-enhanced solid-state NMR determined spatial distributions of organic functionalities attached to surfaces of mesoporous silica nanoparticles via co-condensation and grafting.

scholarly journals Spatial distribution of organic functional groups supported on mesoporous silica nanoparticles (2): a study by 1H triple-quantum fast-MAS solid-state NMR

2018 ◽  
Vol 20 (34) ◽  
pp. 22203-22209 ◽  
Author(s):  
Takeshi Kobayashi ◽  
Dilini Singappuli-Arachchige ◽  
Igor I. Slowing ◽  
Marek Pruski
Keyword(s):  
Spatial Distribution ◽  
Solid State ◽  
Mesoporous Silica ◽  
Silica Nanoparticles ◽  
Solid State Nmr ◽  
Quantum Correlation ◽  
Mesoporous Silica Nanoparticles ◽  
Single Quantum ◽  
Organic Functional Groups ◽  
Fast Mas

Spatial distribution of organic functionalities deposited on mesoporous silica with low loading was determined by 1H triple-quantum/single quantum correlation solid-state NMR.

scholarly journals Characterization of functional groups in estuarine dissolved organic matter by DNP‐enhanced 15N and 13C solid‐state NMR

ChemPhysChem ◽  
2021 ◽  
Author(s):  
Florian Venel ◽  
Hiroki Nagashima ◽  
Andrew G.M. Rankin ◽  
Christelle Anquetil ◽  
Vytautas Klimavicius ◽  
...  
Keyword(s):  
Organic Matter ◽  
Solid State ◽  
Dissolved Organic Matter ◽  
Functional Groups ◽  
Solid State Nmr

Solid state NMR of membrane proteins: methods and applications

2021 ◽  
Author(s):  
Vivien Yeh ◽  
Boyan B. Bonev
Keyword(s):  
Solid State ◽  
High Resolution ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Lipid Membrane ◽  
Cell Function ◽  
Membrane Lipid ◽  
Pharmacological Intervention ◽  
Nmr Methods ◽  
Informative Approach

Membranes of cells are active barriers, in which membrane proteins perform essential remodelling, transport and recognition functions that are vital to cells. Membrane proteins are key regulatory components of cells and represent essential targets for the modulation of cell function and pharmacological intervention. However, novel folds, low molarity and the need for lipid membrane support present serious challenges to the characterisation of their structure and interactions. We describe the use of solid state NMR as a versatile and informative approach for membrane and membrane protein studies, which uniquely provides information on structure, interactions and dynamics of membrane proteins. High resolution approaches are discussed in conjunction with applications of NMR methods to studies of membrane lipid and protein structure and interactions. Signal enhancement in high resolution NMR spectra through DNP is discussed as a tool for whole cell and interaction studies.

Protein structure by solid-state NMR spectroscopy

1987 ◽  
Vol 19 (1-2) ◽  
pp. 7-49 ◽  
Author(s):  
S. J. Opella ◽  
P. L. Stewart ◽  
K. G. Valentine
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Structural Information ◽  
Biological Systems ◽  
Genetic Regulation ◽  
Protein Structures ◽  
Crystalline Solid ◽  
Solid State Nmr Spectroscopy ◽  
Nmr Methods

The three-dimensional structures of proteins are among the most valuable contributions of biophysics to the understanding of biological systems (Dickerson & Geis, 1969; Creighton, 1983). Protein structures are utilized in the description and interpretation of a wide variety of biological phenomena, including genetic regulation, enzyme mechanisms, antibody recognition, cellular energetics, and macroscopic mechanical and structural properties of molecular assemblies. Virtually all of the information currently available about the structures of proteins at atomic resolution has been obtained from diffraction studies of single crystals of proteins (Wyckoff et al, 1985). However, recently developed NMR methods are capable of determining the structures of proteins and are now being applied to a variety of systems, including proteins in solution and other non-crystalline environments that are not amenable for X-ray diffraction studies. Solid-state NMR methods are useful for proteins that undergo limited overall reorientation by virtue of their being in the crystalline solid state or integral parts of supramolecular structures that do not reorient rapidly in solution. For reviews of applications of solid-state NMR spectroscopy to biological systems see Torchia and VanderHart (1979), Griffin (1981), Oldfield et al. (1982), Opella (1982), Torchia (1982), Gauesh (1984), Torchia (1984) and Opella (1986). This review describes how solid-state NMR can be used to obtain structural information about proteins. Methods applicable to samples with macroscopic orientation are emphasized.

scholarly journals Solid-State NMR Techniques for the Structural Characterization of Cyclic Aggregates Based on Borane–Phosphane Frustrated Lewis Pairs

Molecules ◽  
2020 ◽  
Vol 25 (6) ◽  
pp. 1400 ◽  
Author(s):  
Robert Knitsch ◽  
Melanie Brinkkötter ◽  
Thomas Wiegand ◽  
Gerald Kehr ◽  
Gerhard Erker ◽  
...  
Keyword(s):  
Solid State ◽  
Structural Characterization ◽  
Solid State Nmr ◽  
Magic Angle ◽  
Frustrated Lewis Pairs ◽  
Wide Range ◽  
Nmr Techniques ◽  
Nmr Methods ◽  
Lewis Pairs

Modern solid-state NMR techniques offer a wide range of opportunities for the structural characterization of frustrated Lewis pairs (FLPs), their aggregates, and the products of cooperative addition reactions at their two Lewis centers. This information is extremely valuable for materials that elude structural characterization by X-ray diffraction because of their nanocrystalline or amorphous character, (pseudo-)polymorphism, or other types of disordering phenomena inherent in the solid state. Aside from simple chemical shift measurements using single-pulse or cross-polarization/magic-angle spinning NMR detection techniques, the availability of advanced multidimensional and double-resonance NMR methods greatly deepened the informational content of these experiments. In particular, methods quantifying the magnetic dipole–dipole interaction strengths and indirect spin–spin interactions prove useful for the measurement of intermolecular association, connectivity, assessment of FLP–ligand distributions, and the stereochemistry of adducts. The present review illustrates several important solid-state NMR methods with some insightful applications to open questions in FLP chemistry, with a particular focus on supramolecular associates.

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