▪ Abstract Comparative modeling predicts the three-dimensional structure of a given protein
sequence (target) based primarily on its alignment to one or more proteins of known …

Artificial intelligence (AI) in the form of deep learning has promise for drug discovery and
chemical biology, for example, to predict protein structure and molecular bioactivity, plan …

Structural genomics seeks to expand rapidly the number of protein structures in order to
extract the maximum amount of information from genomic sequence databases. The advent …

To assess whether there are universal rules that govern amino acid–base recognition, we
investigate hydrogen bonds, van der Waals contacts and water-mediated bonds in 129 …

Intrinsic protein disorder refers to segments or to whole proteins that fail to fold completely
on their own. Here we predicted disorder on protein sequences from 34 genomes, including …

We present an analysis of the residues directly involved in catalysis in 178 enzyme active
sites. Specific criteria were derived to define a catalytic residue, and used to create a …

The term “starch-binding domain”(SBD) has been applied to a domain within an amylolytic
enzyme that gave the enzyme the ability to bind onto raw, ie thermally untreated, granular …

The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of
Escherichia coli. Here we show that GroEL interacts strongly with a well-defined set of …

Background A large number of studies have been carried out to obtain amino acid
propensities for α-helices and β-sheets. The obtained propensities for α-helices are …

Abstract The SWISS‐MODEL Repository is a database of annotated three‐dimensional
comparative protein structure models generated by the fully automated homology‐modelling …