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Structure, Function and Dynamics in Proteins 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 30 June 2024 | Viewed by 1261

Special Issue Editor


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Guest Editor
Department of Environmental, Biological and Pharmaceutical Science and Technology, University of Campania Luigi Vanvitelli, Via Antonio Vivaldi 43, 81100 Caserta, Italy
Interests: nuclear magnetic resonance spectroscopy; protein structure and dynamics; protein folding and misfolding; metal-binding protein; conformational equilibria; neurodegenerative diseases
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Special Issue Information

Dear Colleagues,

This Special Issue continues on from the previous edition, “Structure, Function and Dynamics in Proteins”.

The structure–dynamics–function relationship plays crucial roles in the biological function of proteins. High-resolution protein structures can currently be obtained from X-ray crystallography (X-ray), nuclear magnetic resonance (NMR) and cryo-electron microscopy (Cryo-EM) techniques, as well as, under certain conditions, computer molecular modeling. Sometimes, three-dimensional protein structures fail to give a complete understanding of the concerned functional mechanisms. Protein dynamics and conformational transitions, in most biological functions, are the essential link that connects high-resolution structural details with cellular processes ranging from protein folding, enzymatic catalysis to signaling, solute transport and synaptic transmission. Over the last decades, experimental techniques such as NMR relaxation, fluorescence spectroscopy, time-resolved X-ray and molecular dynamics have made substantial progress in providing an accurate description, at an atomic level, of protein dynamics on timescales of nano- and microseconds. Moreover, recent progress in the experimental and theoretical methodologies has expanded the scope of research into understanding the interplay between protein structural dynamics and functions for folded and intrinsically disordered proteins. This Special Issue of IJMS aims to make a substantial contribution to the understanding of protein structural dynamics and functional relationships by publishing innovative studies in the fields of protein structural dynamics and protein functions. We encourage researchers to submit original papers covering technical development, experimental studies on some specific proteins, clinical studies with biomolecules and theoretical research, as well as review articles relating to the topic.

Dr. Luigi Russo
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • protein structure and dynamics
  • protein–protein and protein–DNA interactions
  • protein folding and misfolding
  • protein aggregation processes
  • intermediate/misfolded states
  • conformational equilibria
  • DNA and ligand recognition mechanisms
  • membrane receptors
  • enzyme dynamics
  • metal-binding proteins
  • intrinsically disordered proteins
  • cell signaling
  • phase separation mechanims
  • solution- and solid-state nmr
  • molecular dynamics simulations
  • time-resolved X-ray
  • NMR relaxation
  • in-/on-cell NMR
  • Cryo-EM
  • fluorescence polarization
  • surface plasmon resonance
  • static and dynamic light scattering
  • isothermal titration calorimetry
  • microscale thermophoresis
  • protein–fragment complementation assay
  • cross-linking
  • protein microarray

Published Papers (1 paper)

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Review

18 pages, 2526 KiB  
Review
Emerging Roles of B56 Phosphorylation and Binding Motif in PP2A-B56 Holoenzyme Biological Function
by Yanqiao Zhang, Haonan Jiang, Haimeng Yin, Xinyuan Zhao and Yali Zhang
Int. J. Mol. Sci. 2024, 25(6), 3185; https://doi.org/10.3390/ijms25063185 - 10 Mar 2024
Viewed by 751
Abstract
Protein serine/threonine phosphatase 2A (PP2A) regulates diverse cellular processes via the formation of ~100 heterotrimeric holoenzymes. However, a scarcity of knowledge on substrate recognition by various PP2A holoenzymes has greatly prevented the deciphering of PP2A function in phosphorylation-mediated signaling in eukaryotes. The review [...] Read more.
Protein serine/threonine phosphatase 2A (PP2A) regulates diverse cellular processes via the formation of ~100 heterotrimeric holoenzymes. However, a scarcity of knowledge on substrate recognition by various PP2A holoenzymes has greatly prevented the deciphering of PP2A function in phosphorylation-mediated signaling in eukaryotes. The review summarized the contribution of B56 phosphorylation to PP2A-B56 function and proposed strategies for intervening B56 phosphorylation to treat diseases associated with PP2A-B56 dysfunction; it especially analyzed recent advancements in LxxIxEx B56-binding motifs that provide the molecular details of PP2A-B56 binding specificity and, on this basis, explored the emerging role of PP2A-B56 in the mitosis process, virus attack, and cancer development through LxxIxE motif-mediated PP2A-B56 targeting. This review provides theoretical support for discriminatingly targeting specific PP2A holoenzymes to guide PP2A activity against specific pathogenic drivers. Full article
(This article belongs to the Special Issue Structure, Function and Dynamics in Proteins 2.0)
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