A kinetic model for enzyme interfacial activity and stability: pa-hydroxynitrile lyase at the diisopropyl ether/water interface.
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Solvent-amino acid interaction energies in three-dimensional-lattice Monte Carlo simulations of a model 27-mer protein: Folding thermodynamics and kineticsInterfacial versus homogeneous enzymatic cleavage of mandelonitrile by hydroxynitrile lyase in a biphasic system.Evaluating endoglucanase Cel7B-lignin interaction mechanisms and kinetics using quartz crystal microgravimetry.Adsorption of comb copolymers on weakly attractive solid surfaces.
P2860
A kinetic model for enzyme interfacial activity and stability: pa-hydroxynitrile lyase at the diisopropyl ether/water interface.
description
2002 nî lūn-bûn
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2002年の論文
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2002年学术文章
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name
A kinetic model for enzyme int ...... opropyl ether/water interface.
@en
A kinetic model for enzyme int ...... opropyl ether/water interface.
@nl
type
label
A kinetic model for enzyme int ...... opropyl ether/water interface.
@en
A kinetic model for enzyme int ...... opropyl ether/water interface.
@nl
prefLabel
A kinetic model for enzyme int ...... opropyl ether/water interface.
@en
A kinetic model for enzyme int ...... opropyl ether/water interface.
@nl
P2093
P2860
P356
P1476
A kinetic model for enzyme int ...... opropyl ether/water interface.
@en
P2093
Andrea Hickel
Clayton J Radke
Harvey W Blanch
Luis G Cascão Pereira
P2860
P304
P356
10.1002/BIT.10241
P577
2002-06-01T00:00:00Z