Results 101 to 110 of about 23,171 (195)
A Unifying Thermodynamic Model for Phase Separation and Aging of Biopolymers
Advanced Science, Volume 13, Issue 57, 14 October 2026.Phase separation and aging of intrinsically disordered proteins are placed in a unifying framework. A thermodynamically consistent time‐dependent version of associating‐polymer theory shows how the processes are intricately coupled. Assuming aging to occur through interacting sites resulting from reversible conformational transitions, the model ...
Jasper J. Michels +2 more
wiley +1 more source
Sizes, conformational fluctuations, and SAXS profiles for Intrinsically Disordered Proteins
bioRxivThe preponderance of Intrinsically Disordered Proteins (IDPs) in the eukaryotic proteome, and their ability to interact with each other, folded proteins, RNA, and DNA for functional purposes, have made it important to quantitatively characterize their ...
M. Mugnai +8 more
semanticscholar +1 more source
Generalized design of sequence-ensemble-function relationships for intrinsically disordered proteins
bioRxivThe design of folded proteins has advanced significantly in recent years. However, many proteins and protein regions are intrinsically disordered (IDPs) and lack a stable fold i.e., the sequence of an IDP encodes a vast ensemble of spatial conformations ...
R. Krueger +2 more
semanticscholar +1 more source
How to drug a cloud? Targeting intrinsically disordered proteins.
Pharmacological ReviewsBiologically active proteins/regions without stable structure (i.e., intrinsically disordered proteins and regions (IDPs and IDRs)) are commonly found in all proteomes.
V. Uversky
semanticscholar +1 more source
Structural disorder of plasmid-encoded proteins in Bacteria and Archaea
BMC Bioinformatics, 2018 Background In the last decade and a half it has been firmly established that a large number of proteins do not adopt a well-defined (ordered) structure under physiological conditions.
Nenad S. Mitić +4 more
doaj +1 more source
Frontiers in BiophysicsIntrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) lack stable tertiary structures yet perform essential roles in cellular signaling, molecular recognition, transcriptional regulation, and biomolecular assembly.
Rahul Kaushik, Suyong Re
doaj +1 more source
Martini3-IDP: improved Martini 3 force field for disordered proteins
Nature CommunicationsCoarse-grained (CG) molecular dynamics (MD) is widely used for the efficient simulation of intrinsically disordered proteins (IDPs). The Martini model, one of the most popular CG force fields in biomolecular simulation, was reported to yield too compact ...
Li-Guo Wang +4 more
semanticscholar +1 more source
Recent Advances in Computational Protocols Addressing Intrinsically Disordered Proteins
Biomolecules, 2019 Intrinsically disordered proteins (IDP) are abundant in the human genome and have recently emerged as major therapeutic targets for various diseases. Unlike traditional proteins that adopt a definitive structure, IDPs in free solution are disordered and ...
Supriyo Bhattacharya, Xingcheng Lin
doaj +1 more source
A proline switch explains kinetic heterogeneity in a coupled folding and binding reaction
Nature Communications, 2018 How intrinsically disordered proteins (IDPs) undergo a coupled folding and binding reaction with their molecular targets remains to be understood. Here authors use single-molecule FRET to assess the contribution of cis/trans isomerization of peptidyl ...
Franziska Zosel +3 more
doaj +1 more source
Diffusion-limited association of disordered protein by non-native electrostatic interactions
Nature Communications, 2018 Intrinsically disordered proteins (IDPs) usually fold during binding to target proteins which involves the formation of a transient complex (TC). Here authors use single-molecule FRET to show that the lifetime of TC for IDP binding is very long due to ...
Jae-Yeol Kim +3 more
doaj +1 more source