Results 21 to 30 of about 23,171 (195)
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
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Adenosine triphosphate as a modulator of protein interactions and stability. [PDF]
FEBS Open BioATP 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 ...
Tan S, Curtis R.
europepmc +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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IDP-LM: Prediction of protein intrinsic disorder and disorder functions based on language models
PLOS Computational Biology, 2023 Intrinsically disordered proteins (IDPs) and regions (IDRs) are a class of functionally important proteins and regions that lack stable three-dimensional structures under the native physiologic conditions. They participate in critical biological processes and thus are associated with the pathogenesis of many severe human diseases.
Yihe Pang, Bin Liu
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Biomolecules, 2022 Research in previous decades has shown that intrinsically disordered proteins (IDPs) and regions in proteins (IDRs) are as ubiquitous as highly ordered proteins. Despite this, research on IDPs and IDRs still has many gaps left to fill.
Miloš Avramov +7 more
doaj +1 more source
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
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How multisite phosphorylation impacts the conformations of intrinsically disordered proteins.
PLoS Computational Biology, 2021 Phosphorylation of intrinsically disordered proteins (IDPs) can produce changes in structural and dynamical properties and thereby mediate critical biological functions.
Fan Jin, Frauke Gräter
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The Amazing World of IDPs in Human Diseases II
Biomolecules, 2022 Intrinsically Disordered Proteins (IDPs) lack stable tertiary and secondary structures and are extensively distributed across eukaryotic cells, playing critical roles in cell signaling and regulation [...]
Simona Maria Monti +2 more
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Biophysical and Structural Study of Intrinsically Disordered Protein (IDP), Nopp140 [PDF]
Biophysical Journal, 2013 Human Nopp140 is a highly phosphorylated nucleolus protein and involved in the biogenesis of the nucleolus. It interacts with a variety of proteins related to the synthesis and assembly of the ribosome including a ubiquitous protein kinase CK2 which mediates cell growth and prevents apoptosis.
Na, Jung-Hyun +4 more
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Molecules, 2021 Intrinsically disordered proteins (IDPs) are critical players in the dynamic control of diverse cellular processes, and provide potential new drug targets because their dysregulation is closely related to many diseases.
Yusuke Hosoya, Junko Ohkanda
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