Results 61 to 70 of about 23,171 (195)
Biomolecules, 2022 The unique functions of intrinsically disordered proteins (IDPs) depend on their dynamic protean structure that often eludes analysis. High-speed atomic force microscopy (HS-AFM) can conduct this difficult analysis by directly visualizing individual IDP ...
Toshio Ando
doaj +1 more source
bioRxiv, 2022 The formation and viscoelastic properties of condensates of intrinsically disordered proteins (IDPs) is dictated by amino acid sequence and solution conditions.
G. Tesei, K. Lindorff-Larsen
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
semanticscholar +1 more source
Emerging experimental and computational methods for studying redox‐regulated structural transitions
FEBS Letters, EarlyView.Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass +2 more
wiley +1 more source
Frontiers in Molecular Biosciences, 2014 Biologically active proteins without stable tertiary structure are common in all known proteomes. Functions of these intrinsically disordered proteins (IDPs) are typically related to regulation, signaling and control.
Vladimir N. Uversky
doaj +1 more source
FEBS Letters, EarlyView.Transient oligomers formed by intrinsically disordered proteins may be ‘invisible’ to direct detection yet remain accessible to solution NMR through equilibrium‐exchange measurements and pressure‐jump experiments. Complementary methods report on mass, stoichiometry, selected distance distributions, morphology, and internal packing.
Martin D. Gelenter, Ad Bax
wiley +1 more source
Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities. [PDF]
PLoS Computational Biology, 2016 The properties of disordered proteins are thought to depend on intrinsic conformational propensities for polyproline II (PPII) structure. While intrinsic PPII propensities have been measured for the common biological amino acids in short peptides, the ...
Maria E Tomasso +3 more
doaj +1 more source
Orchestrating vesicular and nonvesicular membrane dynamics by intrinsically disordered proteins
EMBO Reports, 2023 Compartmentalization by membranes is a common feature of eukaryotic cells and serves to spatiotemporally confine biochemical reactions to control physiology.
S. Sigrist, V. Haucke
semanticscholar +1 more source
Nature CommunicationsDetermining accurate atomic resolution conformational ensembles of intrinsically disordered proteins (IDPs) is extremely challenging. Molecular dynamics (MD) simulations provide atomistic conformational ensembles of IDPs, but their accuracy is highly ...
Kaushik Borthakur +4 more
semanticscholar +2 more sources
Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy
Biomolecules, 2020 Elucidating the structural details of proteins is highly valuable and important for the proper understanding of protein function. In the case of intrinsically disordered proteins (IDPs), however, obtaining the structural details is quite challenging, as ...
Do-Hyoung Kim +4 more
doaj +1 more source