Angewandte Chemie (International ed. in English)
Oct 10, 2017
Many intrinsically disordered proteins (IDP) that fold upon binding retain conformational heterogeneity in IDP-target complexes. The thermodynamics of such fuzzy interactions is poorly understood. Herein we introduce a thermodynamic framework, based ...
BACKGROUND: Intrinsically Disordered Proteins (IDPs) lack an ordered three-dimensional structure and are enriched in various biological processes. The Molecular Recognition Features (MoRFs) are functional regions within IDPs that undergo a disorder-t...
International journal of molecular sciences
Oct 26, 2016
Information about the interface sites of Protein-Protein Interactions (PPIs) is useful for many biological research works. However, despite the advancement of experimental techniques, the identification of PPI sites still remains as a challenging tas...
We introduce a new representation and feature extraction method for biological sequences. Named bio-vectors (BioVec) to refer to biological sequences in general with protein-vectors (ProtVec) for proteins (amino-acid sequences) and gene-vectors (Gene...
Intrinsically disordered proteins or, regions perform important biological functions through their dynamic conformations during binding. Thus accurate identification of these disordered regions have significant implications in proper annotation of fu...
Molecular dynamics (MD) simulations are fundamental for probing the structural dynamics of biomolecules, yet their efficiency is limited by the high computational cost of exploring long-timescale events. Generative machine learning (ML) models, parti...
Interactions between proteins and lipids are crucial for numerous cellular processes. Some of the lipid interacting segments in protein sequences are intrinsically disordered regions (IDRs), which may gain secondary structures upon binding. We collec...
Undruggable targets are those of therapeutical significance but challenging for conventional drug design approaches. Such targets often exhibit unique features, including highly dynamic structures, a lack of well-defined ligand-binding pockets, the p...
Whereas alignment has been fundamental to sequence-based assessments of protein homology, it is ineffective for intrinsically disordered regions (IDRs) due to their lowered sequence conservation and unique sequence properties. Here, we present a web ...
Journal of chemical information and modeling
May 26, 2025
Interactions between intrinsically disordered proteins (IDPs) are crucial for biological processes, such as intracellular liquid-liquid phase separation (LLPS). Experiments (e.g., NMR) and simulations used to study IDP interactions encounter a variet...
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