Results 21 to 30 of about 5,123 (214)
The lifestyle switch protein Bd0108 of Bdellovibrio bacteriovorus is an intrinsically disordered protein. [PDF]
PLoS ONE, 2014 Bdellovibrio bacteriovorus is a δ-proteobacterium that preys upon Salmonella spp., E. coli, and other Gram-negative bacteria. Bdellovibrio can grow axenically (host-independent, HI, rare and mutation-driven) or subsist via a predatory lifecycle (host ...
Gerd Prehna +2 more
doaj +3 more sources
Journal of Materials Chemistry B, 2015 Data source: Supplementary information, http://www.rsc.org/suppdata/c5/tb/c5tb00659g/c5tb00659g1.pdfHerein we demonstrate the green synthesis of fluorescent gold nanoclusters (AuNCs) using a multiresponsive intrinsically disordered protein (IDP) polymer,
Balu, R. +5 more
core +6 more sources
The Journal of Physical Chemistry BIntrinsically Disordered Proteins (IDPs) constitute a large and structure-less class of proteins with significant functions. The existence of IDPs challenges the conventional notion that the biological functions of proteins rely on their three ...
Mollaei, Parisa +3 more
core +3 more sources
Role of charges in a dynamic disordered complex between an IDP and a folded domain
Nature CommunicationsProtein complexes involving intrinsically disordered proteins (IDPs) cover a continuum from IDPs that fully fold upon binding to IDPs that remain fully disordered in the complex. Here we demonstrate a case of charge-driven interactions of a folded domain
Katrine Bugge +10 more
doaj +2 more sources
Intrinsically disordered proteins (IDPs) in trypanosomatids [PDF]
BMC Genomics, 2014 Proteins are composed of one or more amino acid chains and exhibit several structure levels. IDPs (intrinsically disordered proteins) represent a class of proteins that do not fold into any particular conformation and exist as dynamic ensembles in their native state.
Ruy, Patrícia +5 more
openaire +2 more sources
Biomolecules, 2022 Research in previous decades has shown that intrinsically disordered proteins (IDPs) and regions in proteins (IDRs) are as ubiquitous as highly ordered proteins. Despite this, research on IDPs and IDRs still has many gaps left to fill.
Miloš Avramov +7 more
doaj +1 more source
Structural Analysis of Intrinsically Disordered Protein (IDP): TRIOBP [PDF]
Biophysical Journal, 2014 TRIOBP is an actin-bundling protein. Mutations of TRIOBP are associated with human deafness DFNB28. TRIOBP has three isoforms, named TRIOBP-1, TRIOBP-4, and TRIOBP-5. In vitro, TRIOBP isoform 4 (TRIOBP-4) forms dense F-actin bundles resembling the inner ear hair cell rootlet structure.
Gunther, Laura K. +4 more
openaire +1 more source
Unraveling the Thermodynamics of Ultra-tight Binding of Intrinsically Disordered Proteins
Frontiers in Molecular Biosciences, 2021 Protein interactions mediated by the intrinsically disordered proteins (IDPs) are generally associated with lower affinities compared to those between globular proteins.
Uroš Zavrtanik, San Hadži, Jurij Lah
doaj +1 more source
Novel Strategies for Drug Discovery Based on Intrinsically Disordered Proteins (IDPs) [PDF]
International Journal of Molecular Sciences, 2011 Intrinsically disordered proteins (IDPs) are proteins that usually do not adopt well-defined native structures when isolated in solution under physiological conditions. Numerous IDPs have close relationships with human diseases such as tumor, Parkinson disease, Alzheimer disease, diabetes, and so on.
Jihua Wang +3 more
openaire +4 more sources
Journal of Genetic Engineering and Biotechnology, 2023 Background Hepatitis E virus (HEV) is the cause of a liver disease hepatitis E. The translation product of HEV ORF2 has recently been demonstrated as a protein involved in multiple functions besides performing its major role of a viral capsid.
Zoya Shafat +3 more
doaj +1 more source