The molecular basis for cellular function of intrinsically disordered protein regions
AS Holehouse, BB Kragelund - Nature Reviews Molecular Cell Biology, 2024 - nature.com
Intrinsically disordered protein regions exist in a collection of dynamic interconverting
conformations that lack a stable 3D structure. These regions are structurally heterogeneous …
conformations that lack a stable 3D structure. These regions are structurally heterogeneous …
[HTML][HTML] Biomolecular NMR spectroscopy in the era of artificial intelligence
Biomolecular nuclear magnetic resonance (NMR) spectroscopy and artificial intelligence
(AI) have a burgeoning synergy. Deep learning-based structural predictors have forever …
(AI) have a burgeoning synergy. Deep learning-based structural predictors have forever …
PED in 2024: improving the community deposition of structural ensembles for intrinsically disordered proteins
Abstract The Protein Ensemble Database (PED)(URL: https://proteinensemble. org) is the
primary resource for depositing structural ensembles of intrinsically disordered proteins. This …
primary resource for depositing structural ensembles of intrinsically disordered proteins. This …
Design of intrinsically disordered protein variants with diverse structural properties
Intrinsically disordered proteins (IDPs) perform a broad range of functions in biology,
suggesting that the ability to design IDPs could help expand the repertoire of proteins with …
suggesting that the ability to design IDPs could help expand the repertoire of proteins with …
Direct prediction of intrinsically disordered protein conformational properties from sequence
Intrinsically disordered regions (IDRs) are ubiquitous across all domains of life and play a
range of functional roles. While folded domains are generally well-described by a stable 3D …
range of functional roles. While folded domains are generally well-described by a stable 3D …
SOURSOP: A Python package for the analysis of simulations of intrinsically disordered proteins
Conformational heterogeneity is a defining hallmark of intrinsically disordered proteins and
protein regions (IDRs). The functions of IDRs and the emergent cellular phenotypes they …
protein regions (IDRs). The functions of IDRs and the emergent cellular phenotypes they …
A coarse‐grained model for disordered and multi‐domain proteins
Many proteins contain more than one folded domain, and such modular multi‐domain
proteins help expand the functional repertoire of proteins. Because of their larger size and …
proteins help expand the functional repertoire of proteins. Because of their larger size and …
Random, de novo, and conserved proteins: how structure and disorder predictors perform differently
L Middendorf, LA Eicholt - Proteins: Structure, Function, and …, 2024 - Wiley Online Library
Understanding the emergence and structural characteristics of de novo and random proteins
is crucial for unraveling protein evolution and designing novel enzymes. However …
is crucial for unraveling protein evolution and designing novel enzymes. However …
Predicting heteropolymer interactions: Demixing and hypermixing of disordered protein sequences
K Adachi, K Kawaguchi - Physical Review X, 2024 - APS
Cells contain multiple condensates which spontaneously form due to the heterotypic
interactions between their components. Although the proteins and disordered region …
interactions between their components. Although the proteins and disordered region …
Machine-learning-based methods to generate conformational ensembles of disordered proteins
Intrinsically disordered proteins are characterized by a conformational ensemble. While
computational approaches such as molecular dynamics simulations have been used to …
computational approaches such as molecular dynamics simulations have been used to …