The universality of enzymatic rate-temperature dependency.
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Probing the role of highly conserved residues in triosephosphate isomerase--analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzymeThe role of protein dynamics in the evolution of new enzyme functionBiochemistry and Crystal Structure of Ectoine Synthase: A Metal-Containing Member of the Cupin SuperfamilyHarnessing hyperthermostable lactonase from Sulfolobus solfataricus for biotechnological applicationsUnfair competition governs the interaction of pCPI-17 with myosin phosphatase (PP1-MYPT1).Thermostable artificial enzyme isolated by in vitro selection.Cooling reduces cAMP-stimulated exocytosis and adiponectin secretion at a Ca2+-dependent step in 3T3-L1 adipocytesExceptionally large entropy contributions enable the high rates of GTP hydrolysis on the ribosome.Temperature effects on fish production across a natural thermal gradient.Temperature Sensitivity as a Microbial Trait Using Parameters from Macromolecular Rate Theory.Rigidity versus flexibility: the dilemma of understanding protein thermal stability.Testing the Metabolic Theory of Ecology with marine bacteria: Different temperature sensitivity of major phylogenetic groups during the spring phytoplankton bloom.Experimental evolution and the adjustment of metabolic strategies in lactic acid bacteria.Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes.The relief of microtherm inhibition for p-fluoronitrobenzene mineralization using electrical stimulation at low temperatures.Thermodynamic implications of high Q 10 of thermo-TRP channels in living cells.Quantitative time-course metabolomics in human red blood cells reveal the temperature dependence of human metabolic networks.Hyperthermophilic aldolases as biocatalyst for C-C bond formation: rhamnulose 1-phosphate aldolase from Thermotoga maritima.Efficient Fludarabine-Activating PNP From Archaea as a Guidance for Redesign the Active Site of E. Coli PNP.Shuffling Active Site Substate Populations Affects Catalytic Activity: The Case of Glucose Oxidase.Thermoactivation of a cellobiohydrolase.Differences in adaptive dynamics determine the success of virus variants that propagate together.Large scale analysis of protein conformational transitions from aqueous to non-aqueous media.Characterization of the Dihydroorotase from Methanococcus jannaschii.An appraisal of the enzyme stability-activity trade-off.Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.Protein motions and dynamic effects in enzyme catalysis.Dynamic allostery can drive cold adaptation in enzymes.Minimization of dynamic effects in the evolution of dihydrofolate reductase† †Electronic supplementary information (ESI) available: Full experimental procedures; mass spectra of purified proteins; circular dichroism spectra, tabulated experimental dProtein design: from computer models to artificial intelligenceDegradation of Dyes by Laccase
P2860
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P2860
The universality of enzymatic rate-temperature dependency.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
2013年學術文章
@zh-hant
name
The universality of enzymatic rate-temperature dependency.
@en
The universality of enzymatic rate-temperature dependency.
@nl
type
label
The universality of enzymatic rate-temperature dependency.
@en
The universality of enzymatic rate-temperature dependency.
@nl
prefLabel
The universality of enzymatic rate-temperature dependency.
@en
The universality of enzymatic rate-temperature dependency.
@nl
P2093
P1476
The universality of enzymatic rate-temperature dependency.
@en
P2093
Dan S Tawfik
Grzegorz Wieczorek
Shaked Rosenne
P356
10.1016/J.TIBS.2013.11.001
P50
P577
2013-12-05T00:00:00Z