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000049010 0247_ $$2pmid$$apmid:15990960
000049010 0247_ $$2DOI$$a10.1007/s00018-005-5079-2
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000049010 041__ $$aeng
000049010 082__ $$a570
000049010 084__ $$2WoS$$aBiochemistry & Molecular Biology
000049010 084__ $$2WoS$$aCell Biology
000049010 1001_ $$0P:(DE-Juel1)131961$$aFitter, J.$$b0$$uFZJ
000049010 245__ $$aStructural and dynamical features contributing to thermostability in alpha-amylases
000049010 260__ $$aBasel$$bBirkhäuser$$c2005
000049010 300__ $$a1925 - 1937
000049010 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000049010 440_0 $$01153$$aCellular and Molecular Life Sciences$$v62$$x1420-682X
000049010 500__ $$aRecord converted from VDB: 12.11.2012
000049010 520__ $$aIn 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.
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000049010 588__ $$aDataset connected to Web of Science, Pubmed
000049010 650_2 $$2MeSH$$aEnzyme Stability
000049010 650_2 $$2MeSH$$aProtein Conformation
000049010 650_2 $$2MeSH$$aProtein Folding
000049010 650_2 $$2MeSH$$aTemperature
000049010 650_2 $$2MeSH$$aalpha-Amylases: chemistry
000049010 650_7 $$0EC 3.2.1.1$$2NLM Chemicals$$aalpha-Amylases
000049010 650_7 $$2WoSType$$aJ
000049010 65320 $$2Author$$aprotein stability
000049010 65320 $$2Author$$aprotein unfolding
000049010 65320 $$2Author$$aprotein dynamics
000049010 65320 $$2Author$$athermal adaptation
000049010 65320 $$2Author$$aunfolded states
000049010 65320 $$2Author$$aconformational entropy
000049010 773__ $$0PERI:(DE-600)1458497-9$$a10.1007/s00018-005-5079-2$$gVol. 62, p. 1925 - 1937$$p1925 - 1937$$q62<1925 - 1937$$tCellular and molecular life sciences$$v62$$x1420-682X$$y2005
000049010 8567_ $$uhttp://dx.doi.org/10.1007/s00018-005-5079-2
000049010 909CO $$ooai:juser.fz-juelich.de:49010$$pVDB
000049010 9131_ $$0G:(DE-Juel1)FUEK255$$bLeben$$kL01$$lFunktion und Dysfunktion des Nervensystems$$vNeurowissenschaften$$x0
000049010 9141_ $$y2005
000049010 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000049010 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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000049010 980__ $$aI:(DE-Juel1)ICS-6-20110106
000049010 981__ $$aI:(DE-Juel1)IBI-7-20200312
000049010 981__ $$aI:(DE-Juel1)ISB-2-20090406
000049010 981__ $$aI:(DE-Juel1)ICS-6-20110106