Results 11 to 20 of about 40,484 (286)

Intrinsic structural disorder in cytoskeletal proteins. [PDF]

open access: yesCytoskeleton, 2013
Cytoskeleton, the internal scaffold of the cell, displays an exceptional combination of stability and dynamics. It is composed of three major filamentous networks, microfilaments (actin filaments), intermediate filaments (neurofilaments), and ...
Szabó, Beáta   +3 more
core   +5 more sources

Identification of Intrinsically Disordered Proteins and Regions in a Non-Model Insect Species Ostrinia nubilalis (Hbn.)

open access: yesBiomolecules, 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   +2 more sources

Ensemble Docking for Intrinsically Disordered Proteins [PDF]

open access: yesJournal of Chemical Information and Modeling
Abstract Intrinsically disordered proteins (IDPs) are implicated in many human diseases and are increasingly being pursued as drug targets. Conventional structure-based drug design methods that rely on well-defined binding sites are however, largely unsuitable for IDPs.
Anjali Dhar   +2 more
openaire   +4 more sources

Mapping Charge Interactions in Intrinsically Disordered Proteins [PDF]

open access: yesAdvanced Science
Intrinsically disordered proteins (IDPs) are often rich in charged residues, and electrostatic interactions have a pronounced effect on their conformational distributions, interactions and functions.
Michael Phillips   +14 more
doaj   +2 more sources

Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview [PDF]

open access: yesLife, 2020
In recent years, there has been a growing understanding that a significant fraction of the eukaryotic proteome is intrinsically disordered, and that these conformationally dynamic proteins play a myriad of vital biological roles in both normal and ...
Frederik Lermyte
doaj   +2 more sources

Transient tertiary structure in intrinsically disordered proteins revealed by multithermal enhanced sampling [PDF]

open access: yesNature Communications
Intrinsically disordered proteins populate heterogeneous conformational ensembles that are challenging to characterise. While all-atom molecular dynamics simulations can provide detailed insights into dynamic ensembles, achieving sufficient sampling ...
Julian O. Streit   +4 more
doaj   +2 more sources

Intrinsic Fluorescence of Intrinsically Disordered Proteins

open access: yes, 2012
Resolution of the intrinsic emission properties of a protein by different fluorescence spectroscopy techniques is an invaluable tool to detect and characterize its structural architecture and conformational changes under different experimental conditions.
NEYROZ, PAOLO   +3 more
core   +3 more sources

Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders [PDF]

open access: yesFrontiers in Aging Neuroscience, 2015
The recent years have witnessed a rise in the number of intrinsically disordered proteins (IDPs), also known as hybrid proteins, which possess both structured domains and biologically important intrinsically disordered protein regions (IDPRs). These proteins challenge the “one sequence—one structure—one function” concept by demonstrating that the lack ...
Vladimir N. Uversky   +3 more
doaj   +4 more sources

Databases for intrinsically disordered proteins [PDF]

open access: yesActa Crystallographica Section D Structural Biology, 2022
Intrinsically disordered regions (IDRs) lacking a fixed three-dimensional protein structure are widespread and play a central role in cell regulation. Only a small fraction of IDRs have been functionally characterized, with heterogeneous experimental evidence that is largely buried in the literature.
Piovesan, Damiano   +3 more
openaire   +2 more sources

Introducing Protein Intrinsic Disorder [PDF]

open access: yesChemical Reviews, 2014
Central to this model is the notion that the correct shape of the substrate can fit into the active site of the enzyme for enabling an efficient and specific catalysis, as observed for enzymes that hydrolyze β-but not α-glycosidic bonds. 1 Throughout the 20 th century, tens of thousands of structures have been solved and deposited in the Protein Data ...
Habchi, Johnny   +3 more
openaire   +4 more sources

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