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001     49010
005     20200402210034.0
024 7 _ |2 pmid
|a pmid:15990960
024 7 _ |2 DOI
|a 10.1007/s00018-005-5079-2
024 7 _ |2 WOS
|a WOS:000232497400003
024 7 _ |a altmetric:21814534
|2 altmetric
037 _ _ |a PreJuSER-49010
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
084 _ _ |2 WoS
|a Cell Biology
100 1 _ |a Fitter, J.
|b 0
|u FZJ
|0 P:(DE-Juel1)131961
245 _ _ |a Structural and dynamical features contributing to thermostability in alpha-amylases
260 _ _ |a Basel
|b Birkhäuser
|c 2005
300 _ _ |a 1925 - 1937
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Cellular and Molecular Life Sciences
|x 1420-682X
|0 1153
|v 62
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a 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.
536 _ _ |a Neurowissenschaften
|c L01
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK255
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Enzyme Stability
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Protein Folding
650 _ 2 |2 MeSH
|a Temperature
650 _ 2 |2 MeSH
|a alpha-Amylases: chemistry
650 _ 7 |0 EC 3.2.1.1
|2 NLM Chemicals
|a alpha-Amylases
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a protein stability
653 2 0 |2 Author
|a protein unfolding
653 2 0 |2 Author
|a protein dynamics
653 2 0 |2 Author
|a thermal adaptation
653 2 0 |2 Author
|a unfolded states
653 2 0 |2 Author
|a conformational entropy
773 _ _ |a 10.1007/s00018-005-5079-2
|g Vol. 62, p. 1925 - 1937
|p 1925 - 1937
|q 62<1925 - 1937
|0 PERI:(DE-600)1458497-9
|t Cellular and molecular life sciences
|v 62
|y 2005
|x 1420-682X
856 7 _ |u http://dx.doi.org/10.1007/s00018-005-5079-2
909 C O |o oai:juser.fz-juelich.de:49010
|p VDB
913 1 _ |k L01
|v Neurowissenschaften
|l Funktion und Dysfunktion des Nervensystems
|b Leben
|0 G:(DE-Juel1)FUEK255
|x 0
914 1 _ |y 2005
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB58
|x 0
970 _ _ |a VDB:(DE-Juel1)76867
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)ICS-6-20110106

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