(Q27676840)

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Biophysical characterization of mutants ofBacillus subtilislipase evolved for thermostability: Factors contributing to increased activity retention

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Biophysical characterization of mutants ofBacillus subtilislipase evolved for thermostability: Factors contributing to increased activity retention (English)

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5

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4

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object named as

Tjaard Pijning

3

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Manfred T. Reetz

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object named as

Manfred T Reetz

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author name string

Wojciech Augustyniak

1

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Agnieszka A Brzezinska

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Bauke W Dijkstra

6

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publication date

April 2012

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Protein Science

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21

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487-97

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4

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describes a project that uses

1 reference

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Phasercrystallographic software

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VMD: visual molecular dynamics

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Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme

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Protein kinetic stability.

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Directed evolution of enzyme stability

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https://api.crossref.org/works/10.1002%2FPRO.2031

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https://api.crossref.org/works/10.1002%2FPRO.2031

21 January 2018

Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase

1 reference

https://api.crossref.org/works/10.1002%2FPRO.2031

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Stability curves of laboratory evolved thermostable mutants of a Bacillus subtilis lipase

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https://api.crossref.org/works/10.1002%2FPRO.2031

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https://api.crossref.org/works/10.1002%2FPRO.2031

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https://api.crossref.org/works/10.1002%2FPRO.2031

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Thermally denatured state determines refolding in lipase: mutational analysis

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https://api.crossref.org/works/10.1002%2FPRO.2031

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Iterative saturation mutagenesis on the basis of B factors as a strategy for increasing protein thermostability

1 reference

https://api.crossref.org/works/10.1002%2FPRO.2031

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1002/PRO.2031

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