Nuclear magnetic resonance spectroscopy amides

Instmmental methods of analysis provide information about the specific composition and purity of the amines. QuaUtative information about the identity of the product (functional groups present) and quantitative analysis (amount of various components such as nitrile, amide, acid, and deterruination of unsaturation) can be obtained by infrared analysis. Gas chromatography (gc), with a Hquid phase of either Apiezon grease or Carbowax, and high performance Hquid chromatography (hplc), using siHca columns and solvent systems such as isooctane, methyl tert-huty ether, tetrahydrofuran, and methanol, are used for quantitative analysis of fatty amine mixtures. Nuclear magnetic resonance spectroscopy (nmr), both proton ( H) and carbon-13 ( C), which can be used for quaHtative and quantitative analysis, is an important method used to analyze fatty amines (8,81). 

M. Ikura, A. Bax, G. M. Clore and A. M. Gronenborn, Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear 3-dimensional nuclear-magnetic-resonance spectroscopy, J. Am. Chem. Soc., 1990,112, 9020-9022. 

Local structure due to an aromatic-amide interaction observed by proton nuclear magnetic resonance spectroscopy in peptides related to the N terminus of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 230 312-322. 

Primary cultures of neurons, but not astrocytes, contain detectable quantities of a lipid component which we have identified as NAPE by enzymatic cleavage, multiple chromatographic analyses and nuclear magnetic resonance spectroscopy. Neuronal NAPE is composed of a variety of molecular species, which differ in the fatty acyl group bound, through an amide bond, to the ethanolamine moiety of phosphatidylethanolamine (PE). We have found at least five such molecular species in cultured neurons (Table 6.1). 

The stmctural and conformational analysis of proteins adsorbed to solid surfaces is difficult because most common analytical methods are not compatible with the presence of the interacting solids. With recent developments in instrumentation and techniques, our understanding of protein adsorption behavior has improved considerably [4, 14]. The most commonly used techniques include attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR), radiolabeling techniques, immunofluorescence enzyme-linked immunosorbent assay (ELISA), ellipsometry, circular dichroism (CD) spectroscopy, surface plasmon resonance (SPR), and amide HX with nuclear magnetic resonance (NMR). Atomic force microscopy (AFM) and scanning... 

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