Results 11 to 20 of about 448,472 (368)
Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics
Frontiers in Physics, 2019 Recognition of the natural abundance and functional importance of intrinsically disordered proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions (IDPRs) and ordered regions, is changing protein science.
Vladimir N. Uversky, Vladimir N. Uversky
doaj +2 more sources
Intrinsically Disordered Proteins in Chronic Diseases [PDF]
Biomolecules, 2019 It is now increasingly evident that a large fraction of the human proteome comprises proteins that, under physiological conditions, lack fixed, ordered 3D structures as a whole or have segments that are not likely to form a defined 3D structure [...]
Prakash Kulkarni, Vladimir N. Uversky
doaj +5 more sources
Intrinsically Disordered Proteins and the Janus Challenge [PDF]
Biomolecules, 2018 To gain a new insight into the role of proteins in the origin of life on Earth, we present the Janus Challenge: identify an intrinsically disordered protein (IDP), naturally occurring or synthetic, that has catalytic activity.
Prakash Kulkarni, Vladimir N. Uversky
doaj +5 more sources
Templated folding of intrinsically disordered proteins [PDF]
Journal of Biological Chemistry, 2020 Much of our current knowledge of biological chemistry is founded in the structure-function relationship, whereby sequence determines structure that determines function. Thus, the discovery that a large fraction of the proteome is intrinsically disordered,
A. Toto +7 more
semanticscholar +6 more sources
Targeting Intrinsically Disordered Proteins through Dynamic Interactions
Biomolecules, 2020 Intrinsically disordered proteins (IDPs) are over-represented in major disease pathways and have attracted significant interest in understanding if and how they may be targeted using small molecules for therapeutic purposes.
Jianlin Chen, Xiaorong Liu, Jianhan Chen
doaj +2 more sources
PLoS ONE, 2019 Many studies about classification and the functional annotation of intrinsically disordered proteins (IDPs) are based on either the occurrence of long disordered regions or the fraction of disordered residues in the sequence.
Antonio Deiana +3 more
doaj +2 more sources
Artificial intelligence guided conformational mining of intrinsically disordered proteins
Communications Biology, 2022 Generative autoencoders create full conformational ensembles of intrinsically disordered proteins from short molecular dynamics simulations.
Aayush Gupta +3 more
doaj +2 more sources
Intrinsic disorder in putative protein sequences [PDF]
Proteome Science, 2012 Intrinsically disordered proteins (IDPs) and regions (IDRs) perform a variety of crucial biological functions despite lacking stable tertiary structure under physiological conditions in vitro. State-of-the-art sequence-based predictors of intrinsic disorder are achieving per-residue accuracies over 80%.
Uros Midic, Zoran Obradović
openalex +7 more sources
Intrinsically Disordered Proteins in Biomineralization [PDF]
, 2012 Intrinsically disordered proteins (IDPs) have the potential to play a unique role in the study of proteins and the relationships between structure and function. Intrinsic disorder affects chemical and cellular events such as cell signaling, macromolecular self-assembly, protein removal and crystal nucleation and growth.
Magdalena Wojtas +2 more
openalex +4 more sources
Databases for intrinsically disordered proteins [PDF]
Acta 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