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| 001 | 12495 | ||
| 005 | 20200402205928.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:20605671 |
| 024 | 7 | _ | |2 DOI |a 10.1016/j.bpc.2010.05.005 |
| 024 | 7 | _ | |2 WOS |a WOS:000280510000008 |
| 037 | _ | _ | |a PreJuSER-12495 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 540 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 084 | _ | _ | |2 WoS |a Chemistry, Physical |
| 100 | 1 | _ | |a Kumari, A. |b 0 |0 P:(DE-HGF)0 |
| 245 | _ | _ | |a The effect of calcium binding on the unfolding barrier: A kinetic study on homologous a-amylases |
| 260 | _ | _ | |a Amsterdam [u.a.] |b Elsevier Science |c 2010 |
| 300 | _ | _ | |a |
| 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 Biophysical Chemistry |x 0301-4622 |0 9184 |y 1 |v 151 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a 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. |
| 536 | _ | _ | |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |c P45 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK505 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Calcium: chemistry |
| 650 | _ | 2 | |2 MeSH |a Circular Dichroism |
| 650 | _ | 2 | |2 MeSH |a Guanidine: chemistry |
| 650 | _ | 2 | |2 MeSH |a Kinetics |
| 650 | _ | 2 | |2 MeSH |a Protein Binding |
| 650 | _ | 2 | |2 MeSH |a Protein Denaturation |
| 650 | _ | 2 | |2 MeSH |a Protein Stability |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 2 | |2 MeSH |a Temperature |
| 650 | _ | 2 | |2 MeSH |a Thermodynamics |
| 650 | _ | 2 | |2 MeSH |a alpha-Amylases: chemistry |
| 650 | _ | 7 | |0 113-00-8 |2 NLM Chemicals |a Guanidine |
| 650 | _ | 7 | |0 7440-70-2 |2 NLM Chemicals |a Calcium |
| 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 Alpha-amylase |
| 653 | 2 | 0 | |2 Author |a Protein stability |
| 653 | 2 | 0 | |2 Author |a Multi-domain protein |
| 653 | 2 | 0 | |2 Author |a Calcium binding |
| 653 | 2 | 0 | |2 Author |a Thermal unfolding |
| 653 | 2 | 0 | |2 Author |a Eyring-plot |
| 700 | 1 | _ | |a Rosenkranz, T. |b 1 |u FZJ |0 P:(DE-Juel1)VDB72840 |
| 700 | 1 | _ | |a Kayastha, A.M. |b 2 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Fitter, J. |b 3 |u FZJ |0 P:(DE-Juel1)131961 |
| 773 | _ | _ | |a 10.1016/j.bpc.2010.05.005 |g Vol. 151 |q 151 |0 PERI:(DE-600)1496385-1 |t Biophysical chemistry |v 151 |y 2010 |x 0301-4622 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1016/j.bpc.2010.05.005 |
| 909 | C | O | |o oai:juser.fz-juelich.de:12495 |p VDB |
| 913 | 1 | _ | |k P45 |v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |l Biologische Informationsverarbeitung |b Schlüsseltechnologien |0 G:(DE-Juel1)FUEK505 |x 0 |
| 913 | 2 | _ | |a DE-HGF |b Key Technologies |l BioSoft Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences |1 G:(DE-HGF)POF3-550 |0 G:(DE-HGF)POF3-551 |2 G:(DE-HGF)POF3-500 |v Functional Macromolecules and Complexes |x 0 |
| 914 | 1 | _ | |y 2010 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k ISB-2 |l Molekulare Biophysik |d 31.12.2010 |g ISB |0 I:(DE-Juel1)ISB-2-20090406 |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)124119 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 981 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
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