Noncovalent binding provides an invisible wiring diagram for biomolecular pathways and is
the essence of host-guest and supramolecular chemistry. Decades of theoretical and …

Interactions between macromolecules in general, and between proteins in particular, are
essential for any life process. Examples include transfer of information, inhibition or …

Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

Rational drug design is predicated on knowledge of the three-dimensional structure of the
protein− ligand complex and the thermodynamics of ligand binding. Despite the …

Molecular recognition plays a central role in biochemical processes. Although well studied,
understanding the mechanisms of recognition is inherently difficult due to the range of …

Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of proteins
are very common and instrumental for cellular signaling. Recently, a number of studies have …

The human proteome includes many disordered proteins. Although these proteins are
closely linked with a range of human diseases, no clinically approved drug targets them in …

Protein–protein interfaces are considered difficult targets for small-molecule protein–protein
interaction modulators (PPIMs). Here, we present for the first time a computational strategy …

The promiscuous functions of proteins are an important reservoir of functional novelty in
protein evolution, but the molecular basis for binding promiscuity remains elusive. We used …

Introduction Protein thermostability is an important field for its evolutionary perspective of
mesophilic versus thermophilic relationship and for its industrial/therapeutic applications …