Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
-
Englisch
- Bibliographic citation
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In: 10.1002/ange.202101642
- Event
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Veröffentlichung
- (where)
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Aachen
- (who)
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Universitätsbibliothek der RWTH Aachen
- (when)
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2021
- Creator
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Cui, Haiyang
Eltoukhy, Lobna
Zhang, Lingling
Markel, Ulrich
Jaeger, Karl-Erich
Davari, Mehdi D.
Schwaneberg, Ulrich
- DOI
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10.18154/RWTH-2021-04542
- URN
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urn:nbn:de:101:1-2021051303283942353869
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:50 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Cui, Haiyang
- Eltoukhy, Lobna
- Zhang, Lingling
- Markel, Ulrich
- Jaeger, Karl-Erich
- Davari, Mehdi D.
- Schwaneberg, Ulrich
- Universitätsbibliothek der RWTH Aachen
Time of origin
- 2021
Other Objects (12)
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Directed evolution and computational analysis of ionic liquid resistant lipase variants
Engineering of prodigiosin ligase pigC towards production of short-chain prodiginines
CompassR Yields Highly Organic‐Solvent‐Tolerant Enzymes through Recombination of Compatible Substitutions
Polar Substitutions on the Surface of a Lipase Substantially Improve Tolerance in Organic Solvents
Critical assessment of structure-based approaches to improve protein resistance in aqueous ionic liquids by enzyme-wide saturation mutagenesis
Identification of Stable and Enantioselective Lipases for Biotechnological Applications
Engineering of Laccase CueO for Improved Electron Transfer in Bioelectrocatalysis by Semi‐Rational Design
Aqueous ionic liquids redistribute local enzyme stability via long-range perturbation pathways
How to engineer organic solvent resistant enzymes : Insights from combined molecular dynamics and directed evolution study
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Directed evolution and computational analysis of ionic liquid resistant lipase variants
Engineering of prodigiosin ligase pigC towards production of short-chain prodiginines
CompassR Yields Highly Organic‐Solvent‐Tolerant Enzymes through Recombination of Compatible Substitutions
Polar Substitutions on the Surface of a Lipase Substantially Improve Tolerance in Organic Solvents
Critical assessment of structure-based approaches to improve protein resistance in aqueous ionic liquids by enzyme-wide saturation mutagenesis
Identification of Stable and Enantioselective Lipases for Biotechnological Applications
Engineering of Laccase CueO for Improved Electron Transfer in Bioelectrocatalysis by Semi‐Rational Design
Aqueous ionic liquids redistribute local enzyme stability via long-range perturbation pathways
How to engineer organic solvent resistant enzymes : Insights from combined molecular dynamics and directed evolution study
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Directed evolution and computational analysis of ionic liquid resistant lipase variants
Engineering of prodigiosin ligase pigC towards production of short-chain prodiginines
CompassR Yields Highly Organic‐Solvent‐Tolerant Enzymes through Recombination of Compatible Substitutions
Polar Substitutions on the Surface of a Lipase Substantially Improve Tolerance in Organic Solvents
Critical assessment of structure-based approaches to improve protein resistance in aqueous ionic liquids by enzyme-wide saturation mutagenesis
Identification of Stable and Enantioselective Lipases for Biotechnological Applications
Engineering of Laccase CueO for Improved Electron Transfer in Bioelectrocatalysis by Semi‐Rational Design
Aqueous ionic liquids redistribute local enzyme stability via long-range perturbation pathways