Results 31 to 40 of about 2,744,502 (279)

Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology. [PDF]

open access: yesPLoS ONE, 2013
The abundance and potential functional roles of intrinsically disordered regions in aquaporin-4, Kir4.1, a dystrophin isoforms Dp71, α-1 syntrophin, and α-dystrobrevin; i.e., proteins constituting the functional core of the astrocytic dystrophin ...
Insung Na   +5 more
doaj   +1 more source

ReSMAP: Web Server for Predicting Residue-Specific Membrane-Association Propensities of Intrinsically Disordered Proteins

open access: yesMembranes, 2022
The functional processes of many proteins involve the association of their intrinsically disordered regions (IDRs) with acidic membranes. We have identified the membrane-association characteristics of IDRs using extensive molecular dynamics (MD ...
Sanbo Qin   +4 more
doaj   +1 more source

The Intrinsically Disordered Region of ExbD Is Required for Signal Transduction [PDF]

open access: yesJournal of Bacteriology, 2019
The TonB system is a virulence factor for Gram-negative pathogens. The mechanism by which cytoplasmic membrane proteins of the TonB system transduce an electrochemical gradient into mechanical energy is a long-standing mystery. TonB, ExbB, and ExbD primary amino acid sequences are characterized by regions of predicted intrinsic ...
Kopp, Dale R., Postle, Kathleen
openaire   +3 more sources

Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis. [PDF]

open access: yesPLoS Computational Biology, 2009
We perform a large-scale study of intrinsically disordered regions in proteins and protein complexes using a non-redundant set of hundreds of different protein complexes.
Jessica H Fong   +5 more
doaj   +1 more source

Low Complexity Induces Structure in Protein Regions Predicted as Intrinsically Disordered

open access: yesBiomolecules, 2022
There is increasing evidence that many intrinsically disordered regions (IDRs) in proteins play key functional roles through interactions with other proteins or nucleic acids. These interactions often exhibit a context-dependent structural behavior.
Mariane Gonçalves-Kulik   +6 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

Influence of sequence changes and environment on intrinsically disordered proteins. [PDF]

open access: yesPLoS Computational Biology, 2009
Many large-scale studies on intrinsically disordered proteins are implicitly based on the structural models deposited in the Protein Data Bank. Yet, the static nature of deposited models supplies little insight into variation of protein structure and ...
Amrita Mohan   +2 more
doaj   +1 more source

Polycation-π Interactions Are a Driving Force for Molecular Recognition by an Intrinsically Disordered Oncoprotein Family [PDF]

open access: yes, 2013
Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific localized contacts and target-induced disorder to order transitions.
Sheung Chun Ng   +19 more
core   +1 more source

Inferring function using patterns of native disorder in proteins [PDF]

open access: yes, 2007
Natively unstructured regions are a common feature of eukaryotic proteomes. Between 30% and 60% of proteins are predicted to contain long stretches of disordered residues, and not only have many of these regions been confirmed experimentally, but they ...
Swindells, MB   +14 more
core   +2 more sources

Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions

open access: yesBiomolecules, 2022
Intrinsically disordered regions (IDRs) carry out many cellular functions and vary in length and placement in protein sequences. This diversity leads to variations in the underlying compositional biases, which were demonstrated for the short vs. long IDRs. We analyze compositional biases across four classes of disorder: fully disordered proteins; short
Bi Zhao, Lukasz Kurgan
openaire   +3 more sources

Home - About - Disclaimer - Privacy