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@ARTICLE{Kumari:12495,
      author       = {Kumari, A. and Rosenkranz, T. and Kayastha, A.M. and
                      Fitter, J.},
      title        = {{T}he effect of calcium binding on the unfolding barrier:
                      {A} kinetic study on homologous a-amylases},
      journal      = {Biophysical chemistry},
      volume       = {151},
      issn         = {0301-4622},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PreJuSER-12495},
      year         = {2010},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Extreme thermostabilities of proteins can be achieved by
                      binding co-factors to the protein structures. For various
                      alpha-amylases protein stabilization upon calcium binding is
                      a well-known phenomenon. In the present study the mechanism
                      of stabilization of three homologous alpha-amylases was
                      investigated by measuring the unfolding kinetics with CD
                      spectroscopy. For this purpose thermal unfolding kinetics of
                      calcium saturated and calcium depleted enzymes were analyzed
                      by means of Eyring-plots. The free energy change between the
                      native and the transition state which characterized the
                      unfolding barrier height was found to be proportional to the
                      number of calcium ions bound to the protein structures. For
                      the most thermostable alpha-amylases calcium binding caused
                      a significant increase in the enthalpy change, which was
                      partly compensated by increased entropy changes.},
      keywords     = {Calcium: chemistry / Circular Dichroism / Guanidine:
                      chemistry / Kinetics / Protein Binding / Protein
                      Denaturation / Protein Stability / Protein Structure,
                      Tertiary / Temperature / Thermodynamics / alpha-Amylases:
                      chemistry / Guanidine (NLM Chemicals) / Calcium (NLM
                      Chemicals) / alpha-Amylases (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics /
                      Chemistry, Physical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20605671},
      UT           = {WOS:000280510000008},
      doi          = {10.1016/j.bpc.2010.05.005},
      url          = {https://juser.fz-juelich.de/record/12495},
}