Interactions between proteins are orchestrated in a precise and time-dependent manner,
underlying cellular function. The binding affinity, defined as the strength of these …

In recent years, protein science has been revolutionized by the discovery of intrinsically
disordered proteins (IDPs). In contrast to the classical paradigm that a given protein …

Summary β-arrestin plays a key role in G protein-coupled receptor (GPCR) signaling and
desensitization. Despite recent structural advances, the mechanisms that govern receptor-β …

Gene-specific transcription factors (TFs) are key regulatory components of signaling
pathways, controlling, for example, cell growth, development, and stress responses. Their …

G protein-coupled receptors (GPCRs) regulate many cellular and physiological processes,
responding to a diverse range of extracellular stimuli including hormones, neurotransmitters …

The ability of a protein to fold into unique functional state or to stay intrinsically disordered is
encoded in its amino acid sequence. Both ordered and intrinsically disordered proteins …

Many cellular proteins are 'disordered'in isolation. A subset of these intrinsically disordered
proteins (IDPs) can, upon binding another molecule, fold to a well-defined three …

The rates of duplex formation for two octamers of DNA (5′ d-CACGGCTC/5′ d-
GAGCCGTG and 5′ d-CACAGCAC/5′ d-GTGCTGTG), the homologous RNA, and both …

The classical 'lock-and-key'and 'induced-fit'mechanisms for binding both originated in
attempts to explain features of enzyme catalysis. For both of these mechanisms and for their …

Intrinsically disordered proteins (IDPs) are an important class of functional proteins that is
highly prevalent in biology and has broad association with human diseases. In contrast to …