Results 61 to 70 of about 5,123 (214)
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 +4 more
wiley +1 more source
EPR in protein science : intrinsically disordered proteins
, 2011 Intrinsically disordered proteins (IDPs) form a unique protein category characterized by the absence of a well-defined structure and by remarkable conformational flexibility.
Drescher, Malte, Malte Drescher
core +1 more source
Expose flexible conformations for intrinsically disordered protein
Current Research in Structural BiologyThe 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 +8 more
doaj +1 more source
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 +6 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 +4 more
wiley +1 more source
Structural and functional studies of intrinsically disordered fibronectin-binding proteins [PDF]
, 2009 Bacterial fibronectin-binding proteins (FnBPs) mediate adhesion of bacteria to host tissues through binding to the human protein fibronectin (Fn). FnBPs are predicted to contain a series of intrinsically disordered Fn-binding repeats (FnBRs), which ...
Norris, Nicole Catherine
core
Long-lived States in an intrinsically disordered protein domain [PDF]
, 2013 Long-lived states (LLS) are relaxation-favoured eigenstates of J-coupled magnetic nuclei. LLS were measured, along with classical 1H and 15 N relaxation rate constants, in aminoacids of the N-terminal Unique domain of the c-Src kinase (USrc), which is ...
Fernandes, L. +5 more
core +1 more source
Globular and disordered – the non-identical twins in protein-protein interactions
Frontiers in Molecular Biosciences, 2015 In biology proteins from different structural classes interact across and within classes in ways that are optimized to achieve balanced functional outputs.
Kaare eTeilum +2 more
doaj +1 more source
Low-resolution description of the conformational space for intrinsically disordered proteins
Scientific Reports, 2022 Intrinsically disordered proteins (IDP) are at the center of numerous biological processes, and attract consequently extreme interest in structural biology.
Daniel Förster +5 more
doaj +1 more source
Engagement of intrinsic disordered proteins in protein–protein interaction
Frontiers in Molecular Biosciences, 2023 Proteins from the intrinsically disordered group (IDP) focus the attention of many researchers engaged in protein structure analysis. The main criteria used in their identification are lack of secondary structure and significant structural variability ...
Irena Roterman +2 more
doaj +1 more source