This book discusses the paradigm-shifting phenomenon of intrinsically disordered proteins
(IDPs) and hybrid proteins containing ordered domains and functional IDP regions (IDPRs). The
properties of IDPs and IDPRs are highly complementary to those deriving from the presence of a
unique and well-defined three-dimensional fold. Ignored for a long time in high-resolution
studies of proteins intrinsic protein disorder is now recognized as one of the key features
for a large variety of cellular functions where structural flexibility presents a functional
advantage in terms of binding plasticity and promiscuity and this volume explores this exciting
new research.Recent progress in the field has radically changed our perspective to study IDPs
through NMR: increasingly complex IDPs can now be characterized a wide range of observables
can be determined reporting on the structural and dynamic properties computational methods to
describe the structure and dynamics are in continuous development and IDPs can be studied in
environments as complex as whole cells. This volume communicates the new exciting possibilities
offered by NMR and presents open questions to foster further developments.Intrinsically
Disordered Proteins Studied by NMR Spectroscopy provides a snapshot to researchers entering the
field as well as providing a current overview for more experienced scientists in related areas.
