Anmerkungen:
Includes bibliographical references and index
Beschreibung:
"Proteins are fundamental biomolecules in living organisms and play various essential roles. It is composed of twenty amino acid residues connected by amide bonds and forms secondary structures, such as a-helix and b-sheet and ultimately, tertiary structures (Also quaternary structures in the case of protein complex). As the structure of proteins is very important for their function, various methods have been used to analyze them. The first structure clarified was myoglobin, which was reported in 1958 using the X-ray crystallography. Nuclear magnetic resonance spectroscopy has also been highly advanced and widely used for protein structural analysis. Recently, cryoelectron microscopy has also become a powerful tool for the analysis. The structural data is deposited on the "Protein Data Bank" and the number of the solved structure increasing rapidly. As the data can be accessible from all over the world, it supports the progress of the research on protein as well as the development of therapeutics. Recently, the region in protein, which does not assume a particular three dimensional structure, namely, intrinsically disordered region (IDR), has been attracting much attention due to its importance for protein functions. IDR tends to form liquid-liquid separated structure, which provides a site for various biological processes. IDR often receives various post-translational modifications, which are important to modify the function of proteins. In addition, the post-translational modifications often occur heterogeneously. To analyze the structure and function of these regions, the use of the above mentioned methods, such as X-ray crystallography and NMR, are not sufficient, as the regions are highly heterogeneous, mobile and do not have firm tertiary structures. In addition, , the analysis method to identify the site and the kind of the post-translational modification is required to elucidate how these modifications play roles."--