Results 51 to 60 of about 23,829 (240)

Water‐Mediated Phosphoryl Wires Stabilize Pathological Tau Fibrils

open access: yesAngewandte Chemie, EarlyView.
Extended 1D phosphoryl “wires” stabilize in‐register amyloid tau fibrils, as demonstrated by multiple‐quantum spin‐counting NMR, TEM, and MD simulations, using fibrils of tau peptide jR2R3‐P301L (tau295–313) with phosphorylation at S305 or Y310. ABSTRACT Hyperphosphorylation of tau is a hallmark of tauopathies, with specific phosphorylation sites ...
Lokeswara Rao Potnuru   +8 more
wiley   +2 more sources

Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter

open access: yesFrontiers in Genetics, 2018
Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs) are functional proteins and domains that devoid stable secondary and/or tertiary structure.
April L. Darling   +2 more
doaj   +1 more source

New insights into disordered proteins and regions according to the FOD-M model.

open access: yesPLoS ONE, 2022
A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit ...
Irena Roterman   +3 more
doaj   +2 more sources

Creating and Exploiting the Intrinsically Disordered Protein Knowledge Graph (IDP-KG). [PDF]

open access: yes, 2022
There are many data sources containing overlapping information about Intrinsically Disordered Proteins (IDP). IDPcentral aims to be a registry to aid the discovery of data about proteins known to be intrinsically disordered by aggregating the content from these sources. Traditional ETL approaches for populating IDPcentral require the API and data model
Gray, Alasdair   +4 more
openaire   +1 more source

Enzymatic Encoding of Topology in an Intrinsically Disordered Single‐Chain Protein

open access: yesAngewandte Chemie, EarlyView.
Enzymatic intramolecular cross‐linking enables topology control in intrinsically disordered proteins, yielding SCNPs with reproducible cavity architectures. Using β‐casein and microbial transglutaminase, sparse, sequence‐resolved constraints drive compact collapse without inducing secondary structure.
Joshua Johani   +9 more
wiley   +2 more sources

Rapid Fragment Screening by 19F Steady‐State Free Precession NMR

open access: yesAngewandte Chemie, EarlyView.
19F$^{19}{\rm F}$ SSFP NMR is a broadband and very sensitive experiment for detecting protein–ligand interactions. The method enables rapid fragment screening at low micromolar protein concentrations, even for challenging drug targets such as intrinsically disordered proteins.
Laura Ruduša   +8 more
wiley   +2 more sources

Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range

open access: yesbioRxiv, 2022
The formation and viscoelastic properties of condensates of intrinsically disordered proteins (IDPs) is dictated by amino acid sequence and solution conditions.
G. Tesei, K. Lindorff‐Larsen
semanticscholar   +1 more source

Residue packing in globular and intrinsically disordered proteins

open access: yes, 2018
Intrinsically disordered proteins (IDPs)/regions do not have well-defined secondary and tertiary structures, however, they are functional and it is critical to gain a deep understanding of their residue packing. The shape distributions methodology, which
Elife Zerrin Bagci   +3 more
core   +2 more sources

Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics

open access: yesFrontiers in Physics, 2019
Recognition of the natural abundance and functional importance of intrinsically disordered proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions (IDPRs) and ordered regions, is changing protein science.
Vladimir N. Uversky, Vladimir N. Uversky
doaj   +1 more source

The difficulty of aligning intrinsically disordered protein sequences as assessed by conservation and phylogeny.

open access: yesPLoS ONE, 2023
Intrinsically disordered proteins (IDPs) are proteins that lack a stable 3D structure but maintain a biological function. It has been frequently suggested that IDPs are difficult to align because they tend to have fewer conserved residues compared to ...
Andrew C Riley   +2 more
doaj   +1 more source

Home - About - Disclaimer - Privacy