Results 111 to 120 of about 1,763,945 (204)

Structural disorder of plasmid-encoded proteins in Bacteria and Archaea

open access: yesBMC Bioinformatics, 2018
Background In the last decade and a half it has been firmly established that a large number of proteins do not adopt a well-defined (ordered) structure under physiological conditions.
Nenad S. Mitić   +4 more
doaj   +1 more source

Intrinsically disordered regions as drivers of protein aggregation: mechanisms, phase separation, and emerging predictive frameworks

open access: yesFrontiers in Biophysics
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) lack stable tertiary structures yet perform essential roles in cellular signaling, molecular recognition, transcriptional regulation, and biomolecular assembly.
Rahul Kaushik, Suyong Re
doaj   +1 more source

Conformationally adaptive therapeutic peptides for diseases caused by intrinsically disordered proteins (IDPs). New paradigm for drug discovery: Target the target, not the arrow

open access: yesPharmacology & Therapeutics
The traditional model of protein structure determined by the amino acid sequence is today seriously challenged by the fact that approximately half of the human proteome is made up of proteins that do not have a stable 3D structure, either partially or in totality. These proteins, called intrinsically disordered proteins (IDPs), are involved in numerous
Jacques, Fantini   +5 more
  +6 more sources

A proline switch explains kinetic heterogeneity in a coupled folding and binding reaction

open access: yesNature Communications, 2018
How intrinsically disordered proteins (IDPs) undergo a coupled folding and binding reaction with their molecular targets remains to be understood. Here authors use single-molecule FRET to assess the contribution of cis/trans isomerization of peptidyl ...
Franziska Zosel   +3 more
doaj   +1 more source

Recent Advances in Computational Protocols Addressing Intrinsically Disordered Proteins

open access: yesBiomolecules, 2019
Intrinsically disordered proteins (IDP) are abundant in the human genome and have recently emerged as major therapeutic targets for various diseases. Unlike traditional proteins that adopt a definitive structure, IDPs in free solution are disordered and ...
Supriyo Bhattacharya, Xingcheng Lin
doaj   +1 more source

Intrinsically disordered proteins in various hypotheses on the pathogenesis of Alzheimer’xxs and Parkinson’xxs diseases

open access: yes, 2019
"Dancing protein clouds: Intrinsically disordered proteins in the norm and pathology" represents a set of selected studies on a variety of research topics related to intrinsically disordered proteins.
Uversky, Vladimir N.   +1 more
core  

Computational modeling of intrinsically disordered and phase-separated protein states

open access: yes
Intrinsically disordered proteins possess ensembles of conformations and lack stable three-dimensional structures. Phase separation is defined as a phenomenon in which proteins and biomolecules, often including intrinsically disordered proteins, separate
Uversky, Vladimir N.   +1 more
core   +1 more source

IDP-EDL: enhancing intrinsically disordered protein prediction by combining protein language model and ensemble deep learning

open access: yesBriefings in Bioinformatics
Abstract Identification of intrinsically disordered regions (IDRs) in proteins is essential for understanding fundamental cellular processes. The IDRs can be divided into long disordered regions (LDRs) and short disordered regions (SDRs) according to their lengths.
Junxi Xie   +4 more
openaire   +2 more sources

Diffusion-limited association of disordered protein by non-native electrostatic interactions

open access: yesNature Communications, 2018
Intrinsically disordered proteins (IDPs) usually fold during binding to target proteins which involves the formation of a transient complex (TC). Here authors use single-molecule FRET to show that the lifetime of TC for IDP binding is very long due to ...
Jae-Yeol Kim   +3 more
doaj   +1 more source

Characterisation of the effects of intrinsically disordered protein (IDP)-solvent and IDP-lipid interactions in aqueous solution and lipid monolayers

open access: yes, 2019
In dieser Arbeit wurde das Aggregationsverhalten zweier verschiedener Arten intrinsisch unstrukturierter Proteine untersucht. Zum einen wurde der Temperatur-abhängige inverse Phasenübergang von thermoresponsiven Peptid-Polymeren als Funktion der Aminosäuresequenz mit Elektronenspinresonanz- Spektroskopie untersucht.
openaire   +2 more sources

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