Directed evolution converts subtilisin E into a functional equivalent of thermitase

scientific article (publication date: 1999)

Directed evolution converts subtilisin E into a functional equivalent of thermitase is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1093/PROTEIN/12.1.47
P3181OpenCitations bibliographic resource ID787012
P698PubMed publication ID10065710

P2093author name stringH Zhao
F H Arnold
P2860cites workLarge increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfoldingQ27703974
The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'Q27732213
Thermophilic proteins: stability and function in aqueous and organic solventsQ28257251
Directed evolution of enzyme catalystsQ28258199
Mapping the transition state and pathway of protein folding by protein engineeringQ28277014
Molecular evolution by staggered extension process (StEP) in vitro recombinationQ32075357
Protein stability: still an unsolved problemQ33368413
Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1.Q34168280
The sequence of a subtilisin-type protease (aerolysin) from the hyperthermophilic archaeum Pyrobaculum aerophilum reveals sites important to thermostabilityQ36278781
Functional and nonfunctional mutations distinguished by random recombination of homologous genesQ36299795
Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of subtilisin E for catalysis in dimethylformamideQ36366901
Directed evolution of a thermostable esterase.Q36611228
Combinatorial protein design: strategies for screening protein librariesQ36877982
Engineering thermostability: lessons from thermophilic proteinsQ40425159
Prediction and analysis of structure, stability and unfolding of thermolysin-like proteasesQ40775415
Pro-subtilisin E: purification and characterization of its autoprocessing to active subtilisin E in vitroQ41193857
Engineering protein thermal stability. Sequence statistics point to residue substitutions in alpha-helices.Q43018312
Protein thermal stability: hydrogen bonds or internal packing?Q43024795
Protein engineering of disulfide bonds in subtilisin BPN'.Q46822271
Strategies for the in vitro evolution of protein function: enzyme evolution by random recombination of improved sequencesQ46855416
P433issue1
P407language of work or nameEnglishQ1860
P921main subjectdirected evolutionQ440681
P304page(s)47-53
P577publication date1999-01-01
P1433published inProtein Engineering Design and SelectionQ15762396
P1476titleDirected evolution converts subtilisin E into a functional equivalent of thermitase
P478volume12

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