Intrinsically disordered proteins (IDPs) or natively unfolded proteins do not undergo
autonomous folding into a well-defined 3-D structure and challenge the conventional …

Intrinsically disordered proteins (IDPs) can be generally described as a class of proteins that
lack a well-defined ordered structure in isolation at physiological conditions. Upon binding to …

Biologically active but floppy proteins represent a new reality of modern protein science.
These intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered and …

Much of our current knowledge of biological chemistry is founded in the structure-function
relationship, whereby sequence determines structure that determines function. Thus, the …

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 …

Over the past two decades, the prevalence of intrinsically disordered proteins (IDPs) in
biology has become broadly appreciated, which has been paralleled with understanding of …

Intrinsically disordered proteins (IDPs) are highly flexible and undergo disorder to order
transition upon binding. They are highly abundant in human proteomes and play critical …

Sheds new light on intrinsically disordered proteins and peptides, including their role in
neurodegenerative diseases With the discovery of intrinsically disordered proteins and …

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 (IDPs), which in isolation do not adopt a well-defined tertiary
structure but instead populate a structurally heterogeneous ensemble of interconverting …