Intrinsically disordered proteins (IDPs) are characterized by substantial conformational
plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to …

Intrinsically disordered proteins (IDPs) are characterized by highly flexible solvent exposed
backbones and can sample many different conformations. These properties confer them …

Hyperpolarized water can selectively enhance NMR signals of rapidly exchanging protons
in osteopontin (OPN), a metastasis‐associated intrinsically disordered protein (IDP), at near …

The Block V of the RTX domain of the adenylate cyclase protein from Bordetella pertussis is
disordered, and upon binding eight calcium ions, it folds into a beta roll domain with a C …

Uptake of neurotransmitters by sodium-coupled monoamine transporters of the NSS family
is required for termination of synaptic transmission. Transport is tightly regulated by protein …

The conformational ensemble of intrinsically disordered proteins, such as α-synuclein, are
responsible for their function and malfunction. Misfolding of α-synuclein can lead to …

Many properties of intrinsically disordered proteins (IDPs), or protein regions (IDRs), are
modulated by the nature of amino acid side chains as well as by local solvent exposure. We …

Three-dimensional protein structures usually contain regions of local order, called
secondary structure, such as α-helices and β-sheets. Secondary structure is characterized …

Fibril formation of α-synuclein is linked with Parkinson's disease. The intrinsically disordered
nature of α-syn provides extensive conformational plasticity and becomes difficult to …

Function of intrinsically disordered proteins may depend on deviation of their conformational
ensemble from that of a random coil. Such deviation may be hard to characterize and …