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@ARTICLE{Fitter:49010,
      author       = {Fitter, J.},
      title        = {{S}tructural and dynamical features contributing to
                      thermostability in alpha-amylases},
      journal      = {Cellular and molecular life sciences},
      volume       = {62},
      issn         = {1420-682X},
      address      = {Basel},
      publisher    = {Birkhäuser},
      reportid     = {PreJuSER-49010},
      pages        = {1925 - 1937},
      year         = {2005},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {In recent years an increasing number of studies on
                      thermophilic and hyperthermophilic proteins aiming to
                      elucidate determinants of protein thermostability have
                      yielded valuable insights about the relevant mechanisms. In
                      particular, comparison of homologous enzymes with different
                      thermostabilities (isolated from psychrophilic, mesophilic,
                      thermophilic and hyperthermophilic organisms) offers a
                      unique opportunity to determine the strategies of thermal
                      adaptation. In this respect, the medium-sized amylolytic
                      enzyme alpha-amylase is a well-established representative.
                      Various studies on alpha-amylases with very different
                      thermostabilities (melting temperature T(m) = 40-110 degrees
                      C) report structural and dynamical features as well as
                      thermodynamical properties which are supposed to play key
                      roles in thermal adaptation. Here, results from selected
                      homologous alpha-amylases are presented and discussed with
                      respect to some new and recently proposed strategies to
                      achieve thermostability.},
      keywords     = {Enzyme Stability / Protein Conformation / Protein Folding /
                      Temperature / alpha-Amylases: chemistry / alpha-Amylases
                      (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Cell Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15990960},
      UT           = {WOS:000232497400003},
      doi          = {10.1007/s00018-005-5079-2},
      url          = {https://juser.fz-juelich.de/record/49010},
}