Unsupervised learning is becoming an essential tool to analyze the increasingly large
amounts of data produced by atomistic and molecular simulations, in material science, solid …

Protein ubiquitination is a dynamic multifaceted post-translational modification involved in
nearly all aspects of eukaryotic biology. Once attached to a substrate, the 76-amino acid …

Biomolecules are in constant motion. To understand how they function, and why
malfunctions can cause disease, it is necessary to describe their three-dimensional …

The 826 G protein-coupled receptors (GPCRs) in the human proteome regulate key
physiological processes and thus have long been attractive drug targets. With the crystal …

The posttranslational modification with ubiquitin, a process referred to as ubiquitylation,
controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a …

Intrinsically disordered proteins (IDPs) are notoriously challenging to study both
experimentally and computationally. The structure of IDPs cannot be described by a single …

Understanding the structural mechanisms of protein–ligand binding and their dependence
on protein sequence and conformation is of fundamental importance for biomedical …

All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

The protein ubiquitin is a covalent modifier of proteins, including itself. The ubiquitin system
encompasses the enzymes required for catalysing attachment of ubiquitin to substrates as …

By focusing on essential features, while averaging over less important details, coarse-
grained (CG) models provide significant computational and conceptual advantages with …