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Updated: Feb 3, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
Accurate Single-Sequence Prediction of Protein Intrinsic Disorder by an Ensemble of Deep Recurrent and Convolutional
Jack Hanson1, Kuldip Paliwal1, Yaoqi Zhou2
1Signal Processing Laboratory , Griffith University , Brisbane , Queensland 4122 , Australia.
Abstract:
Recognizing the widespread existence of intrinsically disordered regions in proteins spurred the development of computational techniques for their detection. All existing techniques can be classified into methods relying on single-sequence information and those relying on evolutionary sequence profiles generated from multiple-sequence alignments. The methods based on sequence profiles are, in general, more accurate because the presence or absence of conserved amino acid residues in a protein sequence provides important information on the structural and functional roles of the residues. However, the wide applicability of profile-based techniques is limited by time-consuming calculation of sequence profiles. Here we demonstrate that the performance gap between profile-based techniques and single-sequence methods can be reduced by using an ensemble of deep recurrent and convolutional neural networks that allow whole-sequence learning. In particular, the single-sequence method (called SPOT-Disorder-Single) is more accurate than SPOT-Disorder (a profile-based method) for proteins with few homologous sequences and comparable for proteins in predicting long-disordered regions. The method performance is robust across four independent test sets with different amounts of short- and long-disordered regions. SPOT-Disorder-Single is available as a Web server and as a standalone program at http://sparks-lab.org/jack/server/SPOT-Disorder-Single .
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