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000012495 0247_ $$2DOI$$a10.1016/j.bpc.2010.05.005
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000012495 084__ $$2WoS$$aBiochemistry & Molecular Biology
000012495 084__ $$2WoS$$aBiophysics
000012495 084__ $$2WoS$$aChemistry, Physical
000012495 1001_ $$0P:(DE-HGF)0$$aKumari, A.$$b0
000012495 245__ $$aThe effect of calcium binding on the unfolding barrier: A kinetic study on homologous a-amylases
000012495 260__ $$aAmsterdam [u.a.]$$bElsevier Science$$c2010
000012495 300__ $$a
000012495 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000012495 440_0 $$09184$$aBiophysical Chemistry$$v151$$x0301-4622$$y1
000012495 500__ $$aRecord converted from VDB: 12.11.2012
000012495 520__ $$aExtreme 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.
000012495 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x0
000012495 588__ $$aDataset connected to Web of Science, Pubmed
000012495 650_2 $$2MeSH$$aCalcium: chemistry
000012495 650_2 $$2MeSH$$aCircular Dichroism
000012495 650_2 $$2MeSH$$aGuanidine: chemistry
000012495 650_2 $$2MeSH$$aKinetics
000012495 650_2 $$2MeSH$$aProtein Binding
000012495 650_2 $$2MeSH$$aProtein Denaturation
000012495 650_2 $$2MeSH$$aProtein Stability
000012495 650_2 $$2MeSH$$aProtein Structure, Tertiary
000012495 650_2 $$2MeSH$$aTemperature
000012495 650_2 $$2MeSH$$aThermodynamics
000012495 650_2 $$2MeSH$$aalpha-Amylases: chemistry
000012495 650_7 $$0113-00-8$$2NLM Chemicals$$aGuanidine
000012495 650_7 $$07440-70-2$$2NLM Chemicals$$aCalcium
000012495 650_7 $$0EC 3.2.1.1$$2NLM Chemicals$$aalpha-Amylases
000012495 650_7 $$2WoSType$$aJ
000012495 65320 $$2Author$$aAlpha-amylase
000012495 65320 $$2Author$$aProtein stability
000012495 65320 $$2Author$$aMulti-domain protein
000012495 65320 $$2Author$$aCalcium binding
000012495 65320 $$2Author$$aThermal unfolding
000012495 65320 $$2Author$$aEyring-plot
000012495 7001_ $$0P:(DE-Juel1)VDB72840$$aRosenkranz, T.$$b1$$uFZJ
000012495 7001_ $$0P:(DE-HGF)0$$aKayastha, A.M.$$b2
000012495 7001_ $$0P:(DE-Juel1)131961$$aFitter, J.$$b3$$uFZJ
000012495 773__ $$0PERI:(DE-600)1496385-1$$a10.1016/j.bpc.2010.05.005$$gVol. 151$$q151$$tBiophysical chemistry$$v151$$x0301-4622$$y2010
000012495 8567_ $$uhttp://dx.doi.org/10.1016/j.bpc.2010.05.005
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000012495 9131_ $$0G:(DE-Juel1)FUEK505$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x0
000012495 9132_ $$0G:(DE-HGF)POF3-551$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft  Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vFunctional Macromolecules and Complexes$$x0
000012495 9141_ $$y2010
000012495 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000012495 9201_ $$0I:(DE-Juel1)ISB-2-20090406$$d31.12.2010$$gISB$$kISB-2$$lMolekulare Biophysik$$x0
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