Study of the correlation between structural network and structural and catalytic properties of beta-glucosidases (2013)
- Authors:
- USP affiliated authors: MARANA, SANDRO ROBERTO - IQ ; ARANTES, GUILHERME MENEGON - IQ
- Unidade: IQ
- Subjects: PROTEÍNAS; MUTAGÊNESE
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq)
- Publisher place: São Paulo
- Date published: 2013
- Source:
- Título do periódico: Abstracts
- Conference titles: Annual Meeting of the Brazilian Biochemistry and Molecular Biology Society (SBBq)
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ABNT
SOUSA, V P e ARANTES, Guilherme Menegon e MARANA, Sandro Roberto. Study of the correlation between structural network and structural and catalytic properties of beta-glucosidases. 2013, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2013. . Acesso em: 26 abr. 2024. -
APA
Sousa, V. P., Arantes, G. M., & Marana, S. R. (2013). Study of the correlation between structural network and structural and catalytic properties of beta-glucosidases. In Abstracts. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq). -
NLM
Sousa VP, Arantes GM, Marana SR. Study of the correlation between structural network and structural and catalytic properties of beta-glucosidases. Abstracts. 2013 ;[citado 2024 abr. 26 ] -
Vancouver
Sousa VP, Arantes GM, Marana SR. Study of the correlation between structural network and structural and catalytic properties of beta-glucosidases. Abstracts. 2013 ;[citado 2024 abr. 26 ] - Molecular recognition by CDC25B phosphatases
- Protein thermal denaturation is modulated by central residues in the protein structure network
- Role of highly connected residues (hubs) of enzyme structural networks on the substrate specificity
- Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase
- Combining NMR and computer simulations to evaluate Cdc25B protein flexbility
- Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases
- Expression, purification and buffering conditions of Cdc25B for NMR data acquisition
- Ligand binding and conformational dynamics of CDC25B phosphatase
- Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation−π contacts in proteins
- Computational molecular bioenergetics: simulations of iron-sulfur proteins and respiratory complexes
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