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@ARTICLE{Rahban:916060,
      author       = {Rahban, Mahdie and Zolghadri, Samaneh and Salehi, Najmeh
                      and Ahmad, Faizan and Haertlé, Thomas and Rezaie Ghaleh,
                      Nasrollah and Sawyer, Lindsay and Saboury, Ali Akbar},
      title        = {{T}hermal stability enhancement: {F}undamental concepts of
                      protein engineering strategies to manipulate the flexible
                      structure},
      journal      = {International journal of biological macromolecules},
      volume       = {214},
      issn         = {0141-8130},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2022-05906},
      pages        = {642 - 654},
      year         = {2022},
      note         = {Kein Post-Print vorhanden},
      abstract     = {Increasing the temperature by just a few degrees may lead
                      to structural perturbation or unfolding of the protein and
                      consequent loss of function. The concepts of flexibility and
                      rigidity are fundamental for understanding the relationships
                      between function, structure and stability. Protein unfolding
                      can often be triggered by thermal fluctuations with flexible
                      residues usually on the protein surface. Therefore,
                      identification and knowledge of the effect of modification
                      to flexible regions in protein structures are required for
                      efficient protein engineering and the rational design of
                      thermally stable proteins. The most flexible regions in
                      protein are loops, hence their rigidification is one of the
                      effective strategies for increasing thermal stability.
                      Directed evolution or rational design by computational
                      prediction can also lead to the generation of thermally
                      stable proteins. Computational protein design has been
                      improved significantly in recent years and has successfully
                      produced de novo stable backbone structures with optimized
                      sequences and functions. This review discusses
                      intramolecular and intermolecular interactions that
                      determine the protein structure, and the strategies utilized
                      in the mutagenesis of mesophilic proteins to stabilize and
                      improve the functional characteristics of biocatalysts by
                      describing efficient techniques and strategies to rigidify
                      flexible loops at appropriate positions in the structure of
                      the protein.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35772638},
      UT           = {WOS:000861847600003},
      doi          = {10.1016/j.ijbiomac.2022.06.154},
      url          = {https://juser.fz-juelich.de/record/916060},
}