Results 71 to 80 of about 23,829 (240)

Molecular Simulations Integrated with Experiments for Probing the Interaction Dynamics and Binding Mechanisms of Intrinsically Disordered Proteins

Current Opinion in Structural Biology, 2023
Intrinsically disordered proteins (IDPs) exploit their plasticity to deploy a rich panoply of soft interactions and binding phenomena. Advances in tailoring molecular simulations for IDPs combined with experimental cross-validation offer an atomistic ...
Catherine Ghosh, Suhani Nagpal, Victor Muñoz   +2 more
semanticscholar   +1 more source

Intrinsically disordered proteins in various hypotheses on the pathogenesis of Alzheimer's and Parkinson's diseases

, 2019
Amyloid-β (Aβ) and α-synuclein (αS) are two intrinsically disordered proteins (IDPs) at the centers of the pathogenesis of Alzheimer\u27s and Parkinson\u27s diseases, respectively.
Weber, Orkide Coşkuner, Uversky, Vladimir N., Orkid Coskuner, Vladimir N. Uversky, Coskuner, Orkid   +4 more
core   +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

Intramolecular Interactions between Folded and Disordered Regions Shape Ubiquilin Structure and Function

Advanced Science, EarlyView.
Ubiquilin (UBQLN), like many other human proteins, contains both well‐folded and disordered regions. Here, we show that intramolecular interactions between disordered regions and folded domains modulate between open and closed topologies of UBQLN proteins, altering their structure and function.
Jessica K. Niblo, Nirbhik Acharya, Maxwell B. Watkins, Carlos A. Castañeda, Shahar Sukenik   +4 more
wiley   +1 more source

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

, 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

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, Micheal J Tarver, Deepa Devarajan, Steven T Whitten   +3 more
doaj   +1 more source

AI‐Physics‐Experiment Trinity for Integrated Protein Dynamics Modeling

Advanced Science, EarlyView.
This review unites experiments, physics‐based simulations, and AI as a synergistic triad for protein dynamics modeling. It highlights integrative strategies, resolves sampling and forcefield bottlenecks, and outlines challenges and future directions for accurate, interpretable conformational ensemble prediction.
Chen Shi, Minying Low, Peng Xiu, Kresten Lindorff‐Larsen, Yong Wang   +4 more
wiley   +1 more source

Deciphering the mechanisms of binding induced folding at nearly atomic resolution : The Φ value analysis applied to IDPs

, 2014
The Φ value analysis is a method to analyze the structure of metastable states in reaction pathways. Such a methodology is based on the quantitative analysis of the effect of point mutations on the kinetics and thermodynamics of the probed reaction.
Gianni, Stefano, Jemth, Per, Dogan, Jakob, Dogan, Jakob,, Jemth, Per,   +4 more
core   +1 more source

Wrecked regulation of intrinsically disordered proteins in diseases: Pathogenicity of deregulated regulators

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

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, Jongchan Lee, K. H. Mok, Jung Ho Lee, Kyou-Hoon Han   +4 more
doaj   +1 more source