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Research is presented describing studies into the peptide associated with Alzheimer using spectroscopy and segmentation.

1 H NMR was utilized to describe the three-dimensional solution structure of porcine motilin in a membrane-like environment such as the sodium dodecyl sulfate (SDS) micelles. The imaging results have shown that the structure of motilin was characterized by the reverse gamma-turn and a type II beta-turn in the N-terminus, an alpha-helical trait in the middle region, and an extended structure at the C-terminus. The micelle region contained the ampiphilic helical center.

[super 1]H NMR spectroscopy is used for determining the solution structure of the complex formed between the peptide and the fluorophore ReAsH moiety. The biarsenical-tetracysteine motif is used for genetic labeling of proteins with small molecules and the studies have shown that the backbone structure of the peptide is well defined, with a hairpinline turn formed by the central CPGCC segment.

The study aims at new theoretical and experimental approaches to assess the site-to-site variability of the amide (super 15)N CSA parameters in ubiquitin with 76 amino acid residues. The optimal TROSY field for amide nitrogen TROSY is estimated, with only marginal variations due to site-to-site variations.

A study was conducted, using (super 1)H nuclear magnetic resonance (NMR), to investigate the interactions of Alzheimer's amyloid beta-peptide with cyclodextrins. The result reveals that the combined (super 1)H NMR diffusion and chemical shift changes can be used to quantitatively determine affinities and stoichiometries of weak interactions, using unlabeled ligands and hosts of comparable sizes.