% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Duy:49011,
      author       = {Duy, C. and Fitter, J.},
      title        = {{T}hermostability of {I}rreversible {U}nfolding
                      alpha-{A}mylases {A}nalyzed by {U}nfolded {K}inetics},
      journal      = {The journal of biological chemistry},
      volume       = {280},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-49011},
      pages        = {37360 - 37365},
      year         = {2005},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {For most multidomain proteins the thermal unfolding
                      transitions are accompanied by an irreversible step, often
                      related to aggregation at elevated temperatures. As a
                      consequence the analysis of thermostabilities in terms of
                      equilibrium thermodynamics is not applicable, at least not
                      if the irreversible process is fast with respect the
                      structural unfolding transition. In a comparative study we
                      investigated aggregation effects and unfolding kinetics for
                      five homologous alpha-amylases, all from mesophilic sources
                      but with rather different thermostabilities. The results
                      indicate that for all enzymes the irreversible process is
                      fast and the precedent unfolding transition is the
                      rate-limiting step. In this case the kinetic barrier toward
                      unfolding, as measured by unfolding rates as function of
                      temperature, is the key feature in thermostability. The
                      investigated enzymes exhibit activation energies (E(a))
                      between 208 and 364 kJmol(-1) and pronounced differences in
                      the corresponding unfolding rates. The most thermostable
                      alpha-amylase from Bacillus licheniformis (apparent
                      transition temperature, T(1/2) approximately 100 degrees C)
                      shows an unfolding rate which is four orders of magnitude
                      smaller as compared with the alpha-amylase from pig pancreas
                      (T(1/2) approximately 65 degrees C). Even with respect to
                      two other alpha-amylases from Bacillus species (T(1/2)
                      approximately 86 degrees C) the difference in unfolding
                      rates is still two orders of magnitude.},
      keywords     = {Animals / Aspergillus oryzae: enzymology / Bacillus:
                      enzymology / Circular Dichroism / Enzyme Stability / Hot
                      Temperature / Kinetics / Protein Denaturation / Protein
                      Folding / Swine / Thermodynamics / Transition Temperature /
                      alpha-Amylases: chemistry / alpha-Amylases: metabolism /
                      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},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16150692},
      UT           = {WOS:000233044500009},
      doi          = {10.1074/jbc.M507530200},
      url          = {https://juser.fz-juelich.de/record/49011},
}