Best claim that we provide no convincing basis to assert that a discrepancy remains between FRET and SAXS results on the dimensions of disordered proteins under physiological conditions. We maintain that a clear discrepancy is apparent in our and other recent publications, including results shown in the Best comment. A plausible origin is fluorophore interactions in FRET experiments.
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http://dx.doi.org/10.1126/science.aar7949 | DOI Listing |
Comput Struct Biotechnol J
December 2024
Department of Computer Science, Virginia Commonwealth University, Richmond, VA 23284, USA.
A large portion of the Intrinsically Disordered Regions (IDRs) in protein sequences interact with proteins, nucleic acids, and other types of ligands. Correspondingly, dozens of sequence-based predictors of binding IDRs were developed. A recently completed second community-based Critical Assessments of protein Intrinsic Disorder prediction (CAID2) evaluated 32 predictors of binding IDRs.
View Article and Find Full Text PDFNat Commun
January 2025
Department for NMR-based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
The pathological deposition of tau and amyloid-beta into insoluble amyloid fibrils are pathological hallmarks of Alzheimer's disease. Molecular chaperones are important cellular factors contributing to the regulation of tau misfolding and aggregation. Here we reveal an Hsp90-independent mechanism by which the co-chaperone p23 as well as a molecular complex formed by two co-chaperones, p23 and FKBP51, modulates tau aggregation.
View Article and Find Full Text PDFGene
January 2025
Department of Biotechnology, Pondicherry Central University, Pondicherry 605014, India.
The PWWP domain is a conserved motif unique to eukaryotes, playing a critical role in various cellular processes. Proteins containing the PWWP domain are typically found in chromatin, where they bind to DNA and histones in nucleosomes, facilitating chromatin-associated functions. Among these proteins, PWWP-domain containing proteins 2A and 2B (PWWP2A and PWWP2B), identified during the H2A interactome analysis, are DNA methyltransferase-related proteins, that are structurally disordered, except for their PWWP domain.
View Article and Find Full Text PDFJ Am Chem Soc
January 2025
Department of Chemistry, Brandeis University, 415 South St., Waltham, Massachusetts 02454, United States.
Despite their critical role in context-dependent interactions for protein functions, intrinsically disordered regions (IDRs) are often overlooked for designing peptide assemblies. Here, we exploit IDRs to enable context-dependent heterotypic assemblies of intrinsically disordered peptides, where "context-dependent" refers to assembly behavior driven by interactions with other molecules. By attaching an aromatic segment to oppositely charged intrinsically disordered peptides, we achieve a nanofiber formation.
View Article and Find Full Text PDFAdv Sci (Weinh)
January 2025
School of Physics, Zhejiang University, Hangzhou, 310058, PR China.
The self-assembly of intrinsically disordered proteins (IDPs) into condensed phases and the formation of membrane-less organelles (MLOs) can be considered as the phenomenon of collective behavior. The conformational dynamics of IDPs are essential for their interactions and the formation of a condensed phase. From a physical perspective, collective behavior and the emergence of phase are associated with long-range correlations.
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