Key points are not available for this paper at this time.
Many proteins and protein segments cannot attain a single stable three-dimensional structure under physiological conditions; instead, they adopt multiple interconverting conformational states. Such intrinsically disordered proteins or protein segments are highly abundant across proteomes, and are involved in various effector functions. This review focuses on different aspects of disordered proteins and disordered protein regions, which form the basis of the so-called "Disorder-function paradigm" of proteins. Additionally, various experimental approaches and computational tools used for characterizing disordered regions in proteins are discussed. Finally, the role of disordered proteins in diseases and their utility as potential drug targets are explored.
Building similarity graph...
Analyzing shared references across papers
Loading...
Rakesh Trivedi
The University of Texas MD Anderson Cancer Center
Hampapathalu Adimurthy Nagarajaram
University of Hyderabad
International Journal of Molecular Sciences
The University of Texas MD Anderson Cancer Center
University of Hyderabad
Building similarity graph...
Analyzing shared references across papers
Loading...
Trivedi et al. (Mon,) studied this question.
synapsesocial.com/papers/6a011dd04716aad0cc85efab — DOI: https://doi.org/10.3390/ijms232214050
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: