Substrate specificity of plant nitrilase complexes is affected by their helical twist
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2399-3642
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
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
- Klassifikation
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Biowissenschaften, Biologie
- Urheber
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Woodward, Jeremy D.
Trompetter, Inga
Sewell, B. Trevor
Piotrowski, Markus
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
-
10.1038/s42003-018-0186-4
- URN
-
urn:nbn:de:101:1-2018121723355227135790
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:48 MESZ
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Beteiligte
- Woodward, Jeremy D.
- Trompetter, Inga
- Sewell, B. Trevor
- Piotrowski, Markus
- SpringerLink (Online service)
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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
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Conformational dynamics and substrate specificity in nutrient transporters
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The origin of the helical twist inversion in single component cholesteric liquid crystals
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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
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Modelling substrate specificity and enantioselectivity for lipases and esterases by substrate-imprinted docking
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Tryptophan synthase complexes: evolution, substrate specificity, and quaternary structure