A thermodynamic study of mesophilic, thermophilic, and hyperthermophilic L-arabinose isomerases: the effects of divalent metal ions on protein stability at elevated temperatures.
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Probing the Folding-Unfolding Transition of a Thermophilic Protein, MTH1880Crystallization and preliminary X-ray crystallographic analysis of L-arabinose isomerase from thermophilic Geobacillus kaustophilus.Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum.Structural insights into conserved L-arabinose metabolic enzymes reveal the substrate binding site of a thermophilic L-arabinose isomerase.
P2860
A thermodynamic study of mesophilic, thermophilic, and hyperthermophilic L-arabinose isomerases: the effects of divalent metal ions on protein stability at elevated temperatures.
description
2005 nî lūn-bûn
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2005年学术文章
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name
A thermodynamic study of mesop ...... lity at elevated temperatures.
@en
A thermodynamic study of mesop ...... lity at elevated temperatures.
@nl
type
label
A thermodynamic study of mesop ...... lity at elevated temperatures.
@en
A thermodynamic study of mesop ...... lity at elevated temperatures.
@nl
prefLabel
A thermodynamic study of mesop ...... lity at elevated temperatures.
@en
A thermodynamic study of mesop ...... lity at elevated temperatures.
@nl
P2093
P2860
P1433
P1476
A thermodynamic study of mesop ...... lity at elevated temperatures.
@en
P2093
Dong-Woo Lee
Eun-Ah Choe
Hae-Hun Shin
Han-Seung Lee
Jong-Won Oh
Sang-Jae Lee
Seong-Bo Kim
Young-Ho Hong
Yu-Ryang Pyun
P2860
P304
P356
10.1016/J.FEBSLET.2005.01.027
P407
P577
2005-01-26T00:00:00Z