Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2.
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Structural features determining thermal adaptation of esterases.Interdomain hydrophobic interactions modulate the thermostability of microbial esterases from the hormone-sensitive lipase familyAn Engineered Version of Human PON2 Opens the Way to Understand the Role of Its Post-Translational Modifications in Modulating Catalytic Activity.Remediating agitation-induced antibody aggregation by eradicating exposed hydrophobic motifs.Detection of Asp371, Phe375, and Tyr376 Influence on GD-95-10 Lipase Using Alanine Scanning Mutagenesis.Extremozymes from metagenome: Potential applications in food processing.Innovative Biocatalysts as Tools to Detect and Inactivate Nerve Agents
P2860
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P2860
Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2.
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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name
Comprehensive analysis of surf ...... lus acidocaldarius esterase 2.
@en
Comprehensive analysis of surf ...... lus acidocaldarius esterase 2.
@nl
type
label
Comprehensive analysis of surf ...... lus acidocaldarius esterase 2.
@en
Comprehensive analysis of surf ...... lus acidocaldarius esterase 2.
@nl
prefLabel
Comprehensive analysis of surf ...... lus acidocaldarius esterase 2.
@en
Comprehensive analysis of surf ...... lus acidocaldarius esterase 2.
@nl
P2860
P50
P356
P1476
Comprehensive analysis of surf ...... lus acidocaldarius esterase 2.
@en
P2093
Margherita Pezzullo
Roberto Nucci
P2860
P356
10.1093/PROTEIN/GZS066
P577
2012-10-03T00:00:00Z