The recent suggestion that the classical structure–function paradigm should be extended to
proteins and protein domains whose native and functional state is intrinsically unstructured …

The experimental material accumulated in the literature on the conformational behavior of
intrinsically unstructured (natively unfolded) proteins was analyzed. Results of this analysis …

The dominant view of protein structure-function is that an amino acid sequence specifies a
three-dimensional (3-D) structure that is a prerequisite for protein function. In contrast, many …

Networks of protein interactions coordinate cellular functions. We describe a bimolecular
fluorescence complementation (BiFC) assay for determination of the locations of protein …

The number of intrinsically disordered proteins known to be involved in cell-signaling and
regulation is growing rapidly. To test for a generalized involvement of intrinsic disorder in …

Natively unfolded or intrinsically unstructured proteins constitute a unique group of the
protein kingdom. The evolutionary persistence of such proteins represents strong evidence …

The dominant view in protein science is that a three-dimensional 3-D) structure is a
prerequisite for protein function. In contrast to this dominant view, there are many …

Publisher Summary This chapter illustrates that protein disorder is encoded by the amino
acid sequence and that protein disorder is essential for many important biological functions …

Publisher Summary Protein folding is a process by which a polypeptide chain acquires its
native structure from an unfolded state through a transition state. Recent studies of the …

The size distribution of molecules within an unfolded state of the N-terminal SH3 domain of
drk (drkN SH3) has been studied by small-angle X-ray scattering (SAXS) and pulsed-field …