The existence and functioning of intrinsically disordered
proteins (IDPs) challenge the classical structure-function paradigm
that equates function with a well-defined 3D structure. Uncovering
the disordered complement of proteomes and understanding their
functioning can extend the structure-function paradigm to herald
new breakthroughs in drug development. Structure and Function of
Intrinsically Disordered Proteins thoroughly covers the history up
to the latest developments in this field.
After examining the principles of protein structure, the
classical paradigm, and the history of structural disorder, the
book focuses on physical techniques for the identification and
characterization of IDPs. It discusses proteomic and bioinformatic
approaches and shows how IDPs behave under crowding conditions in
living cells. The next several chapters describe the structure,
correlating biological processes, and molecular mechanisms of IDPs.
The author also explores the evolutionary advancement of structural
disorder in proteomes and possible ways of extending the
structure-function paradigm to encompass both ordered and
disordered states of proteins. He concludes with discussions on the
involvement of IDPs in various diseases and how to establish
rational drug design through detailed characterization of IDPs.
Although drug discovery rates have leveled off, new insight
generated by the study of IDPs may offer fresh strategies for drug
development. This work illustrates how these proteins defy the
structure-function paradigm and play important regulatory and
signaling roles.
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