Solid-state nuclear magnetic resonance spectroscopy complexes

Wheat starch lysophospholipid forms tiny liposomes in water that could readily be transported into the interior of a starch granule during its development. Solid-state nuclear magnetic resonance spectroscopy suggests that the phospholipids in wheat starch are predominantly complexed with amylose in an amorphous form in the granules.354-356... 

Several interesting review articles have been recently published focusing on the use of NMR methods to study peptide-lipid and small molecular weight molecule interactions in model and natural membranes. Maler as well as Kang and Li highlighted the unique possibilities of solution-state NMR to investigate the structure, dynamics and location of proteins and peptides in artificial bilayers and peptide-lipid interactions. On the other hand, Renault et reviewed recent advances in cellular solid-state nuclear magnetic resonance spectroscopy (SSNMR) to follow the structure, function, and molecular interactions of protein-lipid complexes in their cellular context and at atomic resolution. 

Solid-state nuclear magnetic resonance (NMR) has been extensively used to assess structural properties, electronic parameters and diffusion behavior of the hydride phases of numerous metals and alloys using mostly transient NMR techniques or low-resolution spectroscopy [3]. The NMR relaxation times are extremely useful to assess various diffusion processes over very wide ranges of hydrogen mobility in crystalline and amorphous phases [3]. In addition, several borohydrides [4-6] and alanates [7-11] have also been characterized by these conventional solid-state NMR methods over the years where most attention was on rotation dynamics of the BHT, A1H4, and AlHe anions detection of order-disorder phase transitions or thermal decomposition. There has been little indication of fast long-range diffusion behavior in any complex hydride studied by NMR to date [4-11]. 

Fourier transform infrared spectroscopy was applied to the study of lac resin, a complex natural resin of insect origin, and some of its derivatives. The results obtained by this method are compared with those from earlier studies that used classical methods of chemical analysis. Experiments include the preparation of hard and soft resins, dewaxed lac, ammoniated lac, lac acetal, halogenated lac, hydrolysed lac, rebuilt lac (rebulac), and the preparation of lac metal salts. It is found that FTIR has several advantages over classical methods, but that FTIR data requires supplementing by other instrumental techniques such as FT-Raman spectroscopy and solid state nuclear magnetic resonance. 21 refs. 

Hunger and Wang provide an account of advances in the characterization of solid catalysts in the functioning state by nuclear magnetic resonance spectroscopy. Examples include investigations of zeolite-catalyzed reactions with isotopic labels that allow characterization of transition states and reaction pathways as well as characterization of organic deposits, surface complexes, and reaction intermediates formed in catalyst pores. 

Another way to characterize carbon surfaces is the nondestructive approach by spectroscopy. Some techniques, such as infrared or nuclear magnetic resonance spectroscopy, are well known from classical organic chanistry. The solid state and the complexity of carbon materials require new, deUcate developments of classical spectroscopic methods or call for the use of new nontraditional ones (e.g., x-ray photoelectron spectroscopy). 

Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful method to determine the structure of biomacromolecules and their complexes in solution. It allows determination of the dynamics of proteins, RNA, DNA, and their complexes at atomic resolution. Therefore, NMR spectroscopy can monitor the often transient weak interactions in the interactome of proteins and the interaction between proteins and small-molecule ligands. In addition, intrinsically unstructured proteins can be investigated, and first reports of structure determination of membrane proteins in the immobilized state (solid state) are developing. This review will introduce the fundamental NMR observables as well as the methods to investigate structure and dynamics, and it will discuss several examples where NMR spectroscopy has provided valuable information in the context of Chemical Biology. 

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