Results 61 to 70 of about 448,472 (368)
Glassy dynamics and memory effects in an intrinsically disordered protein construct [PDF]
, 2020 Glassy, nonexponential relaxations in globular proteins are typically attributed to conformational behaviors that are missing from intrinsically disordered proteins. Yet, we show that single molecules of a disordered-protein construct display two signatures of glassy dynamics, logarithmic relaxations and a Kovacs memory effect, in response to changes ...
arxiv +1 more source
mBio, 2020 A distinguishing morphological feature of all herpesviruses is the multiprotein tegument layer located between the nucleocapsid and lipid envelope of the virion. Tegument proteins play multiple roles in viral replication, including viral assembly, but we
Claire M. Metrick +2 more
doaj +1 more source
PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins
Nucleic Acids Research, 2020 The Protein Ensemble Database (PED) (https://proteinensemble.org), which holds structural ensembles of intrinsically disordered proteins (IDPs), has been significantly updated and upgraded since its last release in 2016.
Tamas Lazar +39 more
semanticscholar +1 more source
Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology
Biomolecules, 2023 Intense study of intrinsically disordered proteins (IDPs) did not begin in earnest until the late 1990s when a few groups, working independently, convinced the community that these ‘weird’ proteins could have important functions.
Rachel Evans +3 more
doaj +1 more source
ACS Chemical Neuroscience, 2020 An increasing number of human diseases has been shown to be linked to aggregation and amyloid formation by intrinsically disordered proteins (IDPs). Amylin, amyloid-β, and α-synuclein are, indeed, involved in type-II diabetes, Alzheimer's, and Parkinson ...
M. Sciacca +11 more
semanticscholar +1 more source
Order, Disorder, and Everything in Between
Molecules, 2016 In addition to the “traditional” proteins characterized by the unique crystal-like structures needed for unique functions, it is increasingly recognized that many proteins or protein regions (collectively known as intrinsically disordered proteins (IDPs)
Shelly DeForte, Vladimir N. Uversky
doaj +1 more source
Influence of sequence changes and environment on intrinsically disordered proteins. [PDF]
PLoS 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
Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins
Biomolecules, 2021 Motifs within proteins help us categorize their functions. Intrinsically disordered proteins (IDPs) are rich in short linear motifs, conferring them many different roles.
Estella A. Newcombe +7 more
doaj +1 more source
Intrinsically disordered proteins from A to Z [PDF]
The International Journal of Biochemistry & Cell Biology, 2011 The ideas that proteins might possess specific functions without being uniquely folded into rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of any given proteome would have been considered as a preposterous fiction 15 or even 10 years ago.
unknown ( host institution ) +1 more
openaire +4 more sources
Evolutionarily conserved network properties of intrinsically disordered proteins. [PDF]
PLoS ONE, 2015 Intrinsically disordered proteins (IDPs) lack a stable tertiary structure in isolation. Remarkably, however, a substantial portion of IDPs undergo disorder-to-order transitions upon binding to their cognate partners.
Nivedita Rangarajan +2 more
doaj +1 more source