Protein Disorder

A special issue of Biophysica (ISSN 2673-4125).

Deadline for manuscript submissions: 31 May 2024 | Viewed by 790

Special Issue Editor


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Guest Editor
Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wroclaw, Poland
Interests: bHLH transcription factors; protein localization; protein-protein interaction; protein structure; intrinsically disordered proteins; liquid-liquid phase separation; signal transduction
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Special Issue Information

Dear Colleagues,

The Special Issue, “Protein Disorder”, aims to summarize all aspects of current knowledge concerning the role of intrinsically disordered proteins/regions. This Issue will cover a selection of original and review articles regarding recent studies focused on the role of Intrinsically disordered protein (IDP)/Intrinsically disordered region (IDR) in the context of pathophysiology, leading to different kind of disorders. Experimental and theoretical papers, up-to-date review articles, and commentaries are welcome.

This Issue will cover a selection of original and review articles regarding recent studies focused on the role of Intrinsically disordered proteins (IDsP)/Intrinsically disordered regions (IDRs) in living organism development, health and all other aspects important for the survival and functioning of the organism.

Dr. Beata Greb-Markiewicz
Guest Editor

Manuscript Submission Information

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Keywords

  • protein–protein interaction
  • intrinsically disordered protein
  • intrinsically disordered region
  • membraneless organelles
  • molecular crowding

Published Papers (1 paper)

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10 pages, 869 KiB  
Perspective
Never Fold to Fold Continuously: A Conundrum in Ubiquitin–Proteasome System (UPS)-Mediated Protein Quality Control (PQC)
by Stefano Magnati and Enrico Bracco
Biophysica 2024, 4(2), 158-167; https://doi.org/10.3390/biophysica4020011 - 30 Mar 2024
Viewed by 489
Abstract
In the last few decades, the traditional paradigm of teleonomy, in which the amino acid sequence of a protein is tightly associated with its structure and, in turn, with its function, has been partially undermined. The idea of a protein as a two-state [...] Read more.
In the last few decades, the traditional paradigm of teleonomy, in which the amino acid sequence of a protein is tightly associated with its structure and, in turn, with its function, has been partially undermined. The idea of a protein as a two-state object has been superseded by that of understanding it as a multistate object. Indeed, some proteins, or portions of a protein, display intrinsically disordered regions (IDRs), which means that they lack stable secondary or tertiary structures. While we are aware that IDRs are present in almost half of the total human proteins, we are still quite far away from understanding their contextual-specific functions and figuring out how they mechanistically work. In the present perspective article, we will attempt to summarize the role/s of IDRs in ubiquitin–proteasome system (UPS)-mediated protein quality control (PQC) at different levels, ranging from ubiquitination to protein degradation through the proteasome machinery up to their role in decoding the complex ubiquitin code. Ultimately, we will critically discuss the future challenges we are facing to gain insights into the role of IDRs in regulating UPS-mediated PQC. Full article
(This article belongs to the Special Issue Protein Disorder)
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