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@ARTICLE{Rathi:280723,
      author       = {Rathi, P. C. and Jaeger, Karl-Erich and Gohlke, H.},
      title        = {{S}tructural {R}igidity and {P}rotein {T}hermostability in
                      {V}ariants of {L}ipase {A} from {B}acillus subtilis},
      journal      = {PLoS one},
      volume       = {10},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2016-00480},
      pages        = {e0130289},
      year         = {2015},
      abstract     = {Understanding the origin of thermostability is of
                      fundamental importance in protein biochemistry. Opposing
                      views on increased or decreased structural rigidity of the
                      folded state have been put forward in this context. They
                      have been related to differences in the temporal resolution
                      of experiments and computations that probe atomic mobility.
                      Here, we find a significant (p = 0.004) and fair (R2 = 0.46)
                      correlation between the structural rigidity of a
                      well-characterized set of 16 mutants of lipase A from
                      Bacillus subtilis (BsLipA) and their thermodynamic
                      thermostability. We apply the rigidity theory-based
                      Constraint Network Analysis (CNA) approach, analyzing
                      directly and in a time-independent manner the statics of the
                      BsLipA mutants. We carefully validate the CNA results on
                      macroscopic and microscopic experimental observables and
                      probe for their sensitivity with respect to input
                      structures. Furthermore, we introduce a robust, local
                      stability measure for predicting thermodynamic
                      thermostability. Our results complement work that showed for
                      pairs of homologous proteins that raising the structural
                      stability is the most common way to obtain a higher
                      thermostability. Furthermore, they demonstrate that related
                      series of mutants with only a small number of mutations can
                      be successfully analyzed by CNA, which suggests that CNA can
                      be applied prospectively in rational protein design aimed at
                      higher thermodynamic thermostability.},
      cin          = {IMET},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IMET-20090612},
      pnm          = {89581 - Biotechnology (POF2-89581)},
      pid          = {G:(DE-HGF)POF2-89581},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000358157600033},
      pubmed       = {pmid:26147762},
      doi          = {10.1371/journal.pone.0130289},
      url          = {https://juser.fz-juelich.de/record/280723},
}