Nature achieves differentiation of specific and nonspecific binding in molecular interactions
through precise control of biomolecules in space and time. Artificial systems such as …

Over the past decade, we have observed a massive increase in the amount of information
describing protein sequences from a variety of organisms. 1, 2 While this may reflect the …

The structural states of proteins include ordered globular domains as well as intrinsically
disordered protein regions that exist as highly flexible conformational ensembles in …

Post-translational modifications (PTMs) produce significant changes in the structural
properties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes …

Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …

Proteins are the major component of the living cell. They play crucial roles in the
maintenance of life, and their dysfunctions are known to cause different pathologies. One of …

Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs)
are functional proteins and domains that devoid stable secondary and/or tertiary structure …

It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

Intrinsically disordered proteins (IDPs) play crucial roles in cellular processes and hold
promise as drug targets. However, the dynamic nature of IDPs remains poorly understood …

Intrinsically disordered proteins and intrinsically disordered protein regions are highly
abundant in nature. However, the quantitative and qualitative measures of protein intrinsic …