Results 241 to 250 of about 1,883,575 (282)

Membrane Association of Intrinsically Disordered Proteins. [PDF]

open access: yesAnnu Rev Biophys
MacAinsh M   +3 more
europepmc   +1 more source

Intrinsically Disordered Proteins: An Overview

open access: yesInternational Journal of Molecular Sciences, 2022
Many proteins and protein segments cannot attain a single stable three-dimensional structure under physiological conditions; instead, they adopt multiple interconverting conformational states.
Hampapathalu A Nagarajaram   +1 more
exaly   +4 more sources

Intrinsically Disordered Proteins and Proteins With Intrinsically Disordered Regions in Neurodegenerative Diseases [PDF]

open access: yesBiophysical Reviews, 2022
Many different intrinsically disordered proteins and proteins with intrinsically disordered regions are associated with neurodegenerative diseases. These types of proteins including amyloid-β, tau, α-synuclein, CHCHD2, CHCHD10, and G-protein coupled ...
Orkide Coşkuner-Weber, Vladimir Uversky
exaly   +6 more sources

Intrinsically Disordered Proteins and Biomineralization [PDF]

open access: yesMatrix Biology, 2016
In vertebrates and invertebrates, biomineralization is controlled by the cell and the proteins they produce. A large number of these proteins are intrinsically disordered, gaining some secondary structure when they interact with their binding partners.
Adele L. Boskey, Eduardo Villarreal
exaly   +3 more sources

Classification of Intrinsically Disordered Regions and Proteins

open access: yesChemical Reviews, 2014
1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from a variety of organisms.1,2 While this may reflect the diversity in sequence space, and possibly also in function space,3 a large proportion of the sequences ...
Benjamin Lang   +2 more
exaly   +4 more sources

Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions

Annual Review of Biochemistry, 2014
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid sequences. They recognize proteins, nucleic acids, and other types of partners; they accelerate interactions and chemical reactions between
Christopher J, Oldfield, A Keith, Dunker
openaire   +2 more sources

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