Results 41 to 50 of about 7,902,914 (332)

Evolutionary fine-tuning of residual helix structure in disordered proteins manifests in complex structure and lifetime

open access: yesCommunications Biology, 2023
Evolution-guided mutagenesis and biophysical analysis reveal that residual helical structure in the binding region of an intrinsically disordered protein regulates the lifetime of its complex by affecting its dissociation.
Steffie Elkjær   +6 more
doaj   +1 more source

Hepatitis C Virus Infection and Intrinsic Disorder in the Signaling Pathways Induced by Toll-Like Receptors

open access: yesBiology, 2022
In this study, we examined the interplay between protein intrinsic disorder, hepatitis C virus (HCV) infection, and signaling pathways induced by Toll-like receptors (TLRs).
Elrashdy M. Redwan   +2 more
doaj   +1 more source

An intrinsically disordered region-containing protein mitigates the drought–growth trade-off to boost yields

open access: yesPlant Physiology, 2023
Drought stress poses a serious threat to global agricultural productivity and food security. Plant resistance to drought is typically accompanied by a growth deficit and yield penalty.
Jun Liu   +10 more
semanticscholar   +1 more source

Structural characterization of intrinsically disordered proteins by NMR spectroscopy. [PDF]

open access: yes, 2013
Recent advances in NMR methodology and techniques allow the structural investigation of biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and ...
Contreras-Martos, Sara   +7 more
core   +1 more source

DisoMCS: Accurately Predicting Protein Intrinsically Disordered Regions Using a Multi-Class Conservative Score Approach. [PDF]

open access: yesPLoS ONE, 2015
The precise prediction of protein intrinsically disordered regions, which play a crucial role in biological procedures, is a necessary prerequisite to further the understanding of the principles and mechanisms of protein function.
Zhiheng Wang   +3 more
doaj   +1 more source

The N-terminal intrinsically disordered domain of mgm101p is localized to the mitochondrial nucleoid. [PDF]

open access: yes, 2013
The mitochondrial genome maintenance gene, MGM101, is essential for yeasts that depend on mitochondrial DNA replication. Previously, in Saccharomyces cerevisiae, it has been found that the carboxy-terminal two-thirds of Mgm101p has a functional core ...
George Desmond Clark-Walker (281878)   +12 more
core   +2 more sources

Vesicle Clustering in a Living Synapse Depends on a Synapsin Region that Mediates Phase Separation

open access: yesCell Reports, 2020
Summary: Liquid-liquid phase separation is an increasingly recognized mechanism for compartmentalization in cells. Recent in vitro studies suggest that this organizational principle may apply to synaptic vesicle clusters. Here we test this possibility by
Arndt Pechstein   +8 more
doaj   +1 more source

Mutual induced-fit mechanism drives binding between intrinsically disordered Bim and cryptic binding site of Bcl-xL

open access: yesCommunications Biology, 2023
Dynamic docking simulations reveal the interactions and conformational changes of the intrinsically disordered region of Bim and its cryptic binding site in Bcl-xL, a pro-survival protein involved in cancer progression.
Gert-Jan Bekker   +4 more
doaj   +1 more source

RFPR-IDP: reduce the false positive rates for intrinsically disordered protein and region prediction by incorporating both fully ordered proteins and disordered proteins

open access: yesBriefings Bioinform., 2020
As an important type of proteins, intrinsically disordered proteins/regions (IDPs/IDRs) are related to many crucial biological functions. Accurate prediction of IDPs/IDRs is beneficial to the prediction of protein structures and functions.
Yumeng Liu, Xiaolong Wang, Bin Liu
semanticscholar   +1 more source

pH Induced Switch in the Conformational Ensemble of an Intrinsically Disordered Protein Prothymosin-α and Its Implications to Amyloid Fibril Formation

open access: yesbioRxiv, 2022
Aggregation of intrinsically disordered proteins (IDPs) is the cause of various neu-rodegenerative diseases. Changes in solution pH can trigger IDP aggregation due to a shift in the IDP monomer population with a high aggregation propensity.
Lipika Baidya, G. Reddy
semanticscholar   +1 more source

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