Results 51 to 60 of about 3,579,241 (217)

Connecting the αα-hubs: same fold, disordered ligands, new functions

Cell Communication and Signaling, 2021
Background Signal fidelity depends on protein–protein interaction–‘hubs’ integrating cues from large interactomes. Recently, and based on a common secondary structure motif, the αα-hubs were defined, which are small α-helical domains of large, modular ...
Lasse Staby, Katrine Bugge, Rasmus Greve Falbe-Hansen, Edoardo Salladini, Karen Skriver, Birthe B. Kragelund   +5 more
doaj   +1 more source

Advanced Sampling Methods for Multiscale Simulation of Disordered Proteins and Dynamic Interactions

Biomolecules, 2021
Intrinsically disordered proteins (IDPs) are highly prevalent and play important roles in biology and human diseases. It is now also recognized that many IDPs remain dynamic even in specific complexes and functional assemblies.
Xiping Gong, Yumeng Zhang, Jianhan Chen
doaj   +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, Dana Reichmann, Gábor Erdős   +2 more
wiley   +1 more source

D2P2: database of disordered protein predictions [PDF]

, 2013
We present the Database of Disordered Protein Prediction (D2P2), available at http://d2p2.pro (including website source code). A battery of disorder predictors and their variants, VL-XT, VSL2b, PrDOS, PV2, Espritz and IUPred, were run on all protein ...
Oates, Matt E., Ishida, Takashi, Dosztányi, Zsuzsanna, Romero, Pedro   +3 more
core   +1 more source

Modifications of Lysine Residues 294 and 311 Within the Microtubule‐Binding Region Alter Tau Aggregation and Tubulin Binding Equilibria

Angewandte Chemie, EarlyView.
The molecular consequences of specific lysine modifications in Alzheimer´s disease remain insufficiently resolved in the context of full‐length protein. Here we integrate protein semisynthesis, segmental isotope labelling, and high‐resolution NMR spectroscopy to achieve residue‐resolved interrogation of site‐specific acetylation and carboxymethylation.
Dominik P. Vogl, Mario Migotti, Robert Konrat, Anne C. Conibear, Christian F. W. Becker   +4 more
wiley   +2 more sources

Expose flexible conformations for intrinsically disordered protein

Current Research in Structural Biology
The folding conformation of native protein has flexibility in different degrees, which may bring difficulty in presenting the structures, and also it causes complexity in understanding the relationship between structure and functions.
Jiaan Yang, Wenxin Ji, Wen Xiang Cheng, Gang Wu, Si Tong Sheng, Peng Zhang, Jun Lin, Xiaojia Chen, Qiong Shi   +8 more
doaj   +1 more source

Modulation of the disordered conformational ensembles of the p53 transactivation domain by cancer-associated mutations. [PDF]

PLoS Computational Biology, 2015
Intrinsically disordered proteins (IDPs) are frequently associated with human diseases such as cancers, and about one-fourth of disease-associated missense mutations have been mapped into predicted disordered regions.
Debabani Ganguly, Jianhan Chen
doaj   +1 more source

Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins

Biomolecules, 2022
Intrinsically disordered proteins (IDPs) are ensembles of interconverting conformers whose conformational properties are governed by several physico-chemical factors, including their amino acid composition and the arrangement of oppositely charged ...
Greta Bianchi, Marco Mangiagalli, Alberto Barbiroli, Sonia Longhi, Rita Grandori, Carlo Santambrogio, Stefania Brocca   +6 more
doaj   +1 more source

Invisible but not inaccessible—Revealing transient oligomers formed by intrinsically disordered proteins with solution NMR and complementary methods

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

Adenosine triphosphate as a modulator of protein interactions and stability

FEBS Open Bio, EarlyView.
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley   +1 more source