Thermostability of multidomain proteins: elongation factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and their chimeric forms.
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Experimental evolution of protein-protein interaction networksImmunoproteomic analysis of outer membrane proteins and extracellular proteins of Actinobacillus pleuropneumoniae JL03 serotype 3Conformational change in the C-terminal domain is responsible for the initiation of creatine kinase thermal aggregationInterface matters: the stiffness route to stability of a thermophilic tetrameric malate dehydrogenase.Proteomic analysis provides new insights into the adaptive response of a dinoflagellate Prorocentrum donghaiense to changing ambient nitrogen.Explanation of the stability of thermophilic proteins based on unique micromorphology.Are coarse-grained models apt to detect protein thermal stability? The case of OPEP force field.Guanine nucleotide exchange factor independence of the G-protein eEF1A through novel mutant forms and biochemical properties.Structural and Dynamics Comparison of Thermostability in Ancient, Modern, and Consensus Elongation Factor Tus.
P2860
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P2860
Thermostability of multidomain proteins: elongation factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and their chimeric forms.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
Thermostability of multidomain ...... ilus and their chimeric forms.
@en
Thermostability of multidomain ...... ilus and their chimeric forms.
@nl
type
label
Thermostability of multidomain ...... ilus and their chimeric forms.
@en
Thermostability of multidomain ...... ilus and their chimeric forms.
@nl
prefLabel
Thermostability of multidomain ...... ilus and their chimeric forms.
@en
Thermostability of multidomain ...... ilus and their chimeric forms.
@nl
P2093
P2860
P356
P1433
P1476
Thermostability of multidomain ...... ilus and their chimeric forms.
@en
P2093
Hana Sanderová
Jirí Jonák
Markéta Kepková
Marta Hůlková
Petr Malon
P2860
P356
10.1110/PS.03272504
P577
2004-01-01T00:00:00Z