Results 21 to 30 of about 23,829 (240)
Determining accurate conformational ensembles of intrinsically disordered proteins at atomic resolution [PDF]
Struct DynDetermining 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 ...
Borthakur K +4 more
europepmc +3 more sources
Accurate Generation of Conformational Ensembles for Intrinsically Disordered Proteins with IDPFold. [PDF]
Adv Sci (Weinh)Intrinsically disordered proteins (IDPs) play pivotal roles in various biological functions whose dynamic structures are closely associated with many human diseases, including cancer, diabetes, and Alzheimer disease.
Zhu J +10 more
europepmc +2 more sources
Current Research in Structural BiologyEukaryotic proteins often feature long stretches of amino acids that lack a well-defined three-dimensional structure and are referred to as intrinsically disordered proteins (IDPs) or regions (IDRs).
Snigdha Maiti +4 more
doaj +2 more sources
Intrinsically disordered proteins studied by NMR spectroscopy
Journal of Magnetic Resonance OpenIntrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of complex multi-domain proteins are now identified as a trend topic by the scientific community.
Marco Schiavina +7 more
doaj +3 more sources
idpr: A package for profiling and analyzing Intrinsically Disordered Proteins in R
PLoS ONE, 2022 Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are proteins or protein-domains that do not have a single native structure, rather, they are a class of flexible peptides that can rapidly adopt multiple conformations ...
William M. McFadden, Judith L. Yanowitz
doaj +3 more sources
BMC Molecular and Cell Biology, 2022 Background Intrinsically disordered proteins (IDPs) lack a stable three-dimensional structure under physiological conditions but play crucial roles in many biological processes.
CanZhuang Sun, YongE Feng, GuoLiang Fan
doaj +1 more source
Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins
Biomolecules, 2021 Single molecule fluorescence and nuclear magnetic resonance spectroscopy (NMR) are two very powerful techniques for the analysis of intrinsically disordered proteins (IDPs).
Samuel Naudi-Fabra +2 more
doaj +1 more source
Templated folding of intrinsically disordered proteins [PDF]
, 2020 Much of our current knowledge of biological chemistry is founded in the structure-function relationship, whereby sequence determines structure that determines function. Thus, the discovery that a large fraction of the proteome is intrinsically disordered,
Troilo F. +7 more
core +2 more sources
Structural Analysis of Intrinsically Disordered Protein (IDP): TRIOBP [PDF]
Biophysical Journal, 2014 TRIOBP is an actin-bundling protein. Mutations of TRIOBP are associated with human deafness DFNB28. TRIOBP has three isoforms, named TRIOBP-1, TRIOBP-4, and TRIOBP-5. In vitro, TRIOBP isoform 4 (TRIOBP-4) forms dense F-actin bundles resembling the inner ear hair cell rootlet structure.
Gunther, Laura K. +4 more
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AWSEM-IDP: A Coarse-Grained Force Field for Intrinsically Disordered Proteins [PDF]
The Journal of Physical Chemistry B, 2018 The associative memory, water-mediated, structure and energy model (AWSEM) has been successfully used to study protein folding, binding, and aggregation problems. In this work, we introduce AWSEM-IDP, a new AWSEM branch for simulating intrinsically disordered proteins (IDPs), where the weights of the potentials determining secondary structure formation
Hao Wu +2 more
openaire +2 more sources