SFを中心に生涯1000編を超える作品を執筆し、現在も国内外で人気の「ショートショートの神様」星新一の公式サイトです。

動機Pythonはグラフ描画系のライブラリが豊富です。例えば、matplotlib / seabornpyqtgraphplotlybokehvispyなどがあります。それぞれ長短ある…

Enzymes host active sites inside protein macromolecules, which have diverse, often incredibly complex, and atom-expensive structures. It is an outstanding question what the role of these expensive scaffolds might be in enzymatic catalysis. Answering this question is essential to both enzymology and the design of artificial enzymes with proficiencies that will match those of the best natural enzymes. Protein rigidifying the active site, contrasted with the dynamics and vibrational motion promoting the reaction, as well as long-range electrostatics (also known as electrostatic preorganization) were all proposed as central contributions of the scaffold to the catalysis. Here, we show that all these effects inevitably produce changes in the quantum mechanical electron density in the active site, which in turn defines the reactivity. The phenomena are therefore fundamentally inseparable. The geometry of the electron density–a scalar field characterized by a number of mathematical features such as critical points–is a rigorous and convenient descriptor of enzymatic catalysis and a reporter on the role of the protein. We show how this geometry can be analyzed, linked to the reaction barriers, and report in particular on intramolecular electric fields in enzymes. We illustrate these tools on the studies of electrostatic preorganization in several representative enzyme classes, both natural and artificial. We highlight the forward-looking aspects of the approach.

【NHK】兵庫県姫路市のすし店が作った恵方巻きを食べた34人が下痢やおう吐などを訴えた食中毒で、市の保健所はその後も症状を訴える人…