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Protein Stability Research: 2nd Edition

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

Deadline for manuscript submissions: 25 August 2024 | Viewed by 601

Special Issue Editor


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Guest Editor
Institute of Molecular Life Sciences, HUN-REN Research Centre for Natural Sciences, 1117 Budapest, Hungary
Interests: protein bioinformatics; protein stability; intrinsically disordered proteins; protein structure; protein structure modeling; protein dynamics; molecular dynamics simulation; protein conformation; computational structural biology; structural bioinformatics; drug design; structure based drug design
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Special Issue Information

Dear Colleagues,

Stability is an essential property of protein structures. It can be of crucial importance for the function or regulation of specific proteins. Changing the stability of protein complexes can be a driving force in regulation and communication pathways. Mutations that alter the stability of a protein can lead to diseases through various mechanisms, like diminished function or protein aggregation. Folding intermediates and molten globules can be stabilized by external helping agents, and post-translational modifications can also influence protein stability as a regulation method. A wide repository of experimental and theoretical methods can deal with the problem of protein stability. As Guest Editor of the “Protein Stability Research: 2.0 Edition” Special Issue, I would like to invite you to contribute original articles or reviews related to protein stability.

Dr. Csaba Magyar
Guest Editor

Manuscript Submission Information

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Keywords

  • protein stability
  • protein degradation
  • conformational stability and flexibility
  • thermodynamic stability of proteins
  • mutation-induced changes in protein stability
  • stability of oligomeric proteins
  • stability of protein complexes
  • thermal adaptation of protein structures
  • protein aggregation
  • molten globules
  • heat shock proteins
  • chaperones

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Published Papers (1 paper)

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Research

18 pages, 7967 KiB  
Article
Effect of the Lys62Ala Mutation on the Thermal Stability of BstHPr Protein by Molecular Dynamics
by Aranza C. Martínez-Zacarias, Edgar López-Pérez and Salomón J. Alas-Guardado
Int. J. Mol. Sci. 2024, 25(12), 6316; https://doi.org/10.3390/ijms25126316 - 7 Jun 2024
Viewed by 417
Abstract
We analyzed the thermal stability of the BstHPr protein through the site-directed point mutation Lys62 replaced by Ala residue using molecular dynamics simulations at five different temperatures: 298, 333, 362, 400, and 450 K, for periods of 1 μs and in triplicate. [...] Read more.
We analyzed the thermal stability of the BstHPr protein through the site-directed point mutation Lys62 replaced by Ala residue using molecular dynamics simulations at five different temperatures: 298, 333, 362, 400, and 450 K, for periods of 1 μs and in triplicate. The results from the mutant thermophilic BstHPrm protein were compared with those of the wild-type thermophilic BstHPr protein and the mesophilic BsHPr protein. Structural and molecular interaction analyses show that proteins lose stability as temperature increases. Mutant and wild-type proteins behave similarly up to 362 K. However, at 400 K the mutant protein shows greater structural instability, losing more buried hydrogen bonds and exposing more of its non-polar residues to the solvent. Therefore, in this study, we confirmed that the salt bridge network of the Glu3–Lys62–Glu36 triad, made up of the Glu3–Lys62 and Glu36–Lys62 ion pairs, provides thermal stability to the thermophilic BstHPr protein. Full article
(This article belongs to the Special Issue Protein Stability Research: 2nd Edition)
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