Multi-scale instrumental analyses for structural changes in steam-treated bamboo using a combination of several solid-state NMR methods

2017 ◽  
Vol 103 ◽  
pp. 89-98 ◽  
Author(s):  
Masakazu Nishida ◽  
Tomoko Tanaka ◽  
Tsunehisa Miki ◽  
Takafumi Ito ◽  
Kozo Kanayama
Author(s):  
Vivien Yeh ◽  
Boyan B. Bonev

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.


1987 ◽  
Vol 19 (1-2) ◽  
pp. 7-49 ◽  
Author(s):  
S. J. Opella ◽  
P. L. Stewart ◽  
K. G. Valentine

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.


Molecules ◽  
2020 ◽  
Vol 25 (6) ◽  
pp. 1400 ◽  
Author(s):  
Robert Knitsch ◽  
Melanie Brinkkötter ◽  
Thomas Wiegand ◽  
Gerald Kehr ◽  
Gerhard Erker ◽  
...  

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.


2017 ◽  
Vol 121 (47) ◽  
pp. 26507-26518 ◽  
Author(s):  
Hans J. Jakobsen ◽  
Anders T. Lindhardt ◽  
Henrik Bildsøe ◽  
Jørgen Skibsted ◽  
Zhehong Gan ◽  
...  

2016 ◽  
Vol 6 ◽  
pp. 144-193 ◽  
Author(s):  
Hellmut Eckert

Glassy solid electrolytes are important integral components for all-solid-state devices for energy storage and conversion. The use of multiple network formers is an important part of their design strategy for specific applications. In many glass systems the interaction between the different network formers results in strongly non-linear variations in physical properties (network former mixing (NFM) effects), requiring a detailed understanding on a structural basis.The issues to be addressed involve both the structural organization and connectivities within the framework, the local environments and spatial distributions of the mobile ions, and the dynamical aspects of ion transport, to be discussed in relation to possible phase separation or nano-segregation effects. Besides Raman and X-ray photoelectron spectroscopies, solid state nuclear magnetic resonance (NMR) methods are particularly useful for providing detailed answers to such issues. The present review introduces the basic principles of modern solid state NMR methods and their applications to glass structure, with a particular focus on the characterization of network-former mixing effects in the most common lithium and sodium conducting oxide and chalcogenide glass systems. Based on the current state of the literature reviewed in the present work, some emerging general principles governing structure/property correlations are identified, to be tested by further experimenteation in the future.


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