Israel Silman

TL;DR: Modeling of acetylcholine binding to the enzyme suggests that the quaternary ammonium ion is bound not to a negatively charged "anionic" site, but rather to some of the 14 aromatic residues that line the gorge.

TL;DR: The alpha/beta hydrolase fold as mentioned in this paper is common to several hydrolytic enzymes of widely differing phylogenetic origin and catalytic function, including the serine protease catalytic triad.

TL;DR: Topics concerning proteins inherently lacking 3D structure are discussed, including their prediction from amino acid sequence, their enrichment in eukaryotes compared to prokaryotes, their more rapid evolution compared to structured proteins, their organization into specific groups, their structural preferences, their half-lives in cells, and their involvement in diseases.

TL;DR: An easy-to-use, versatile and freely available graphic web server, FoldIndex© predicts if a given protein sequence is intrinsically unfolded implementing the algorithm of Uversky and co-workers, which is based on the average residue hydrophobicity and net charge of the sequence.

TL;DR: The structural and chemical data show the important role of aromatic groups as binding sites for quaternary ligands in Torpedo acetylcholinesterase, and provide complementary evidence assigning Trp-84 and Phe-330 to the "anionic" subsite of the active site andtrp-279 to the 'peripheral' anionic site.