Results 11 to 20 of about 23,829 (240)
Biomolecules, 2022 The unique functions of intrinsically disordered proteins (IDPs) depend on their dynamic protean structure that often eludes analysis. High-speed atomic force microscopy (HS-AFM) can conduct this difficult analysis by directly visualizing individual IDP ...
Toshio Ando
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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
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INTRINSICALLY DISORDERED PROTEINS (IDPS) IN HUMAN DISEASES: A REVIEW
International Research Journal Of Pharmacy, 2018 Biologically active proteins without stable tertiary structure are called Intrinsically Disordered Proteins (IDPs) or Intrinsically Unstructured Proteins (IUPs).
Divya Shaji
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Structural Characterization of Intrinsically Disordered Proteins by NMR Spectroscopy
Molecules, 2013 Recent advances in NMR methodology and techniques allow the structural investigation of biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and ...
Peter Tompa +3 more
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Intrinsically disordered proteins: controlled chaos or random walk
International Journal of Plant Biology, 2016 Traditional conventions that a protein’s sequence dictates its definitive, tertiary structure, and that this fixed structure provides the protein with the ability to carry out its designated role(s) are still correct but not for all proteins.
T.C. Howton +3 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 Polymers of Life: Exploring Cellular Function Through Polymer Concepts. [PDF]
Adv Sci (Weinh)Biomolecular phase separation reveals that a hidden layer of cellular organization is governed by the principles of polymer science. This review bridges polymer physics and cell biology, offering a primer on fundamental concepts, proposing a framework for interrogating cellular function, and synthesizing biophysical methods for decoding macromolecular ...
Chen M, Chilkoti A.
europepmc +2 more sources
DisProt in 2026: enhancing intrinsically disordered proteins accessibility, deposition, and annotation. [PDF]
Nucleic Acids ResDisProt (https://disprot.org/) is an open database integrating experimental evidence on intrinsically disordered proteins (IDPs), intrinsically disordered regions (IDRs), and their functions.
Nugnes MV +9 more
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CISP, an Intrinsically Disordered Cold-Inducible Barley Protein, Functions as a Small RNA Chaperone. [PDF]
Plant DirectABSTRACT Low temperatures are a major environmental stress that limits plant growth and development. Understanding the molecular mechanism of cold tolerance is therefore essential for improving crop performance through molecular breeding. In this study, we focused on CISP, a small, previously uncharacterized protein, specifically induced in barley ...
Okumura Y, Haque MM, Kidou SI.
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Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology
Biomolecules, 2023 Intense study of intrinsically disordered proteins (IDPs) did not begin in earnest until the late 1990s when a few groups, working independently, convinced the community that these ‘weird’ proteins could have important functions.
Rachel Evans +3 more
semanticscholar +2 more sources