A Sequence-Specific Theory for Charge-Regulating IDPs. [PDF]
Beyer D, Holm C, Wang ZG.
europepmc +1 more source
Folded domains impose structural heterogeneity and attenuated dynamics in biomolecular condensates. [PDF]
Wang L, Marrink SJ.
europepmc +1 more source
Nanopipettes Enable Native Mass Spectrometry Studies of the Intrinsically Disordered Protein α-Synuclein in Biochemical Buffers. [PDF]
Byrd EJ +9 more
europepmc +1 more source
IDPEnsembleTools: An open-source library for analysis of conformational ensembles of disordered proteins. [PDF]
Ghafouri H +3 more
europepmc +1 more source
Alternative Splicing of a Structured Partner Alters the Folding-Upon-Binding Trajectory of an Intrinsically Disordered Protein. [PDF]
Kjaer LF +8 more
europepmc +1 more source
Sequence-Dependent Conformational Landscapes of Intrinsically Disordered Proteins Reveal Asymmetric Chain Compaction. [PDF]
Wang C, Zhang B.
europepmc +1 more source
Hierarchical multi-timescale structural dynamics of the disordered N-terminal of p53. [PDF]
Szöllősi D +13 more
europepmc +1 more source
Extending the MAD Toolbox: New Polymer Builder and Enhanced Martini Database
Marin R +9 more
europepmc +1 more source
openaire +1 more source
IDP–CRF: Intrinsically Disordered Protein/Region Identification Based on Conditional Random Fields [PDF]
Accurate prediction of intrinsically disordered proteins/regions is one of the most important tasks in bioinformatics, and some computational predictors have been proposed to solve this problem. How to efficiently incorporate the sequence-order effect is critical for constructing an accurate predictor because disordered region distributions show global
Xiaolong Wang
exaly +4 more sources

