Results 51 to 60 of about 1,763,945 (204)

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

Unequivocal single-molecule force spectroscopy of intrinsically disordered proteins [PDF]

, 2012
Intrinsically disordered proteins (IDPs) are predicted to represent about one third of the eukaryotic proteome. The dynamic ensemble of conformations of this steadily growing class of proteins has remained hardly accessible for bulk biophysical ...
Rubén Hervás, Carrión-Vázquez, Mariano Sixto, Carrión-Vázquez, Mariano, Oroz, Javier, Valbuena, Alejandro, Hervás, Rubén, Javier Oroz, Alejandro Valbuena, Mariano Carrión-Vázquez   +8 more
core   +1 more source

Actinidia DRM1--an intrinsically disordered protein whose mRNA expression is inversely correlated with spring budbreak in kiwifruit. [PDF]

PLoS ONE, 2013
Intrinsically disordered proteins (IDPs) are a relatively recently defined class of proteins which, under native conditions, lack a unique tertiary structure whilst maintaining essential biological functions.
Marion Wood, Georgina M Rae, Rong-Mei Wu, Eric F Walton, Bin Xue, Roger P Hellens, Vladimir N Uversky   +6 more
doaj   +1 more source

An Evolutionary Algorithm for the Design of Different Degrees of Secondary Structure in Intrinsically Disordered Proteins (IDPs) [PDF]

Biophysical Journal, 2015
In recent experimental studies of coupled folding and binding of IDPs investigators have adapted methods from the protein folding literature whereby point mutations are used to identify the degree to which different regions are pre-folded prior to the rate limiting step in binding and folding. These approaches assume a one-to-one correspondence between
Harmon, Tyler S., Pappu, Rohit V.
openaire   +1 more source

Designing and repurposing drugs to target intrinsically disordered proteins for cancer treatment: using NUPR1 as a paradigm

Molecular & Cellular Oncology, 2019
Intrinsically disordered proteins (IDPs) do not have a well-defined structure, but they have key biological tasks in cancer development. By using the disordered cancer-related protein NUPR1 as a proof-of-concept, we have developed a new multidisciplinary
Patricia Santofimia-Castaño, Bruno Rizzuti, Yi Xia, Olga Abian, Ling Peng, Adrián Velázquez-Campoy, Juan L. Iovanna, José L. Neira   +7 more
doaj   +1 more source

Adenoviral E1A Exploits Flexibility and Disorder to Target Cellular Proteins

Biomolecules, 2020
Direct interaction between intrinsically disordered proteins (IDPs) is often difficult to characterize hampering the elucidation of their binding mechanism.
Maria Grazia Murrali, Isabella C. Felli, Roberta Pierattelli   +2 more
doaj   +1 more source

Deciphering Mode of Action of Functionally Important Regions in the Intrinsically Disordered Paxillin (Residues 1-313) Using Its Interaction with FAT (Focal Adhesion Targeting Domain of Focal Adhesion Kinase). [PDF]

PLoS ONE, 2016
Intrinsically disordered proteins (IDPs) play a major role in various cellular functions ranging from transcription to cell migration. Mutations/modifications in such IDPs are shown to be associated with various diseases.
Muniasamy Neerathilingam, Sneha G Bairy, Sumukh Mysore   +2 more
doaj   +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

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

Development of Charge-Augmented Three-Point Water Model (CAIPi3P) for Accurate Simulations of Intrinsically Disordered Proteins [PDF]

, 2019
Intrinsically disordered proteins (IDPs) are molecules without a fixed tertiary structure, exerting crucial roles in cellular signalling, growth and molecular recognition events. Due to their high plasticity, IDPs are very challenging in experimental and
Agnieszka K., Bronowska, Joao Victor, de Souza Cunha, Francesc, Sabanes Zariquiey   +2 more
core   +1 more source