Substrate specificity of plant nitrilase complexes is affected by their helical twist
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2399-3642
- Extent
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Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Substrate specificity of plant nitrilase complexes is affected by their helical twist ; volume:1 ; number:1 ; day:2 ; month:11 ; year:2018 ; pages:1-10 ; date:12.2018
Communications biology ; 1, Heft 1 (2.11.2018), 1-10, 12.2018
- Classification
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Biowissenschaften, Biologie
- Creator
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Woodward, Jeremy D.
Trompetter, Inga
Sewell, B. Trevor
Piotrowski, Markus
- Contributor
-
SpringerLink (Online service)
- DOI
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10.1038/s42003-018-0186-4
- URN
-
urn:nbn:de:101:1-2018121723355227135790
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:48 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
- Woodward, Jeremy D.
- Trompetter, Inga
- Sewell, B. Trevor
- Piotrowski, Markus
- SpringerLink (Online service)
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Substrate specificity of plant nitrilase complexes is affected by their helical twist
The temperature dependence of the helical twist of DNA
Substrate specificity of human MCPIP1 endoribonuclease
Role of helicity of α-helical antimicrobial peptides to improve specificity
Exploring and engineering the substrate specificity of transaminases
Discovery and substrate specificity engineering of nucleotide halogenases
Conformational dynamics and substrate specificity in nutrient transporters
Quantum Effects Explain the Twist Angle in the Helical Structure of DNA
Modelling substrate specificity and enantioselectivity for lipases and esterases by substrate-imprinted docking
The origin of the helical twist inversion in single component cholesteric liquid crystals
Tryptophan synthase complexes: evolution, substrate specificity, and quaternary structure
The intrinsic substrate specificity of the human tyrosine kinome
Substrate specificity of plant nitrilase complexes is affected by their helical twist
The temperature dependence of the helical twist of DNA
Substrate specificity of human MCPIP1 endoribonuclease
Role of helicity of α-helical antimicrobial peptides to improve specificity
Exploring and engineering the substrate specificity of transaminases
Discovery and substrate specificity engineering of nucleotide halogenases
Conformational dynamics and substrate specificity in nutrient transporters
Quantum Effects Explain the Twist Angle in the Helical Structure of DNA
Modelling substrate specificity and enantioselectivity for lipases and esterases by substrate-imprinted docking
The origin of the helical twist inversion in single component cholesteric liquid crystals
Tryptophan synthase complexes: evolution, substrate specificity, and quaternary structure