In the 1960s, Christian Anfinsen postulated that the unique three-dimensional structure of a
protein is determined by its amino acid sequence. This work laid the foundation for the …

Protein kinases have very dynamic structures and their functionality strongly depends on
their dynamic state. Active kinases reveal a dynamic pattern with residues clustering into …

Motivation After the outstanding breakthrough of AlphaFold in predicting protein 3D models,
new questions appeared and remain unanswered. The ensemble nature of proteins, for …

Understanding signaling and other complex biological processes requires elucidating the
critical roles of intrinsically disordered proteins (IDPs) and regions (IDRs), which represent∼ …

Signaling pathways allow cells to detect and respond to a wide variety of chemical (eg Ca2+
or chemokine proteins) and physical stimuli (eg, sheer stress, light). Together, these …

Intrinsically disordered proteins participate in many important cellular regulatory processes.
The absence of a well-defined structure in the free state of a disordered domain, and even …

The cellular response to hypoxia is critical for cell survival and is fine-tuned to allow cells to
recover from hypoxic stress and adapt to heterogeneous or fluctuating oxygen levels,. The …

Allosteric regulatory processes are implicated at all levels of biological function. Recent
advances in our understanding of the diverse and functionally significant class of intrinsically …

Allostery is a ubiquitous biological regulatory process in which distant binding sites within a
protein or enzyme are functionally and thermodynamically coupled. Allosteric interactions …

Intrinsically disordered proteins must compete for binding to common regulatory targets to
carry out their biological functions. Previously, we showed that the activation domains of two …