Protein thermal denaturation is modulated by central residues in the protein structure network (2016)
- Authors:
- USP affiliated authors: ARANTES, GUILHERME MENEGON - IQ ; MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- DOI: 10.1111/febs.13659
- Subjects: GLICOSÍDEOS; ENZIMAS HIDROLÍTICAS
- Language: Inglês
- Imprenta:
- Source:
- Título: Febs Journal
- ISSN: 1742-464x
- Volume/Número/Paginação/Ano: p. 1-15, 2016
- Status:
- Artigo possui acesso gratuito no site do editor (Bronze Open Access)
- Versão do Documento:
- Versão publicada (Published version)
- Acessar versão aberta:
-
ABNT
SOUZA, Valquiria Pianheri et al. Protein thermal denaturation is modulated by central residues in the protein structure network. Febs Journal, p. 1-15, 2016Tradução . . Disponível em: https://doi.org/10.1111/febs.13659. Acesso em: 09 abr. 2026. -
APA
Souza, V. P., Ikegami, C. M., Arantes, G. M., & Marana, S. R. (2016). Protein thermal denaturation is modulated by central residues in the protein structure network. Febs Journal, 1-15. doi:10.1111/febs.13659 -
NLM
Souza VP, Ikegami CM, Arantes GM, Marana SR. Protein thermal denaturation is modulated by central residues in the protein structure network [Internet]. Febs Journal. 2016 ; 1-15.[citado 2026 abr. 09 ] Available from: https://doi.org/10.1111/febs.13659 -
Vancouver
Souza VP, Ikegami CM, Arantes GM, Marana SR. Protein thermal denaturation is modulated by central residues in the protein structure network [Internet]. Febs Journal. 2016 ; 1-15.[citado 2026 abr. 09 ] Available from: https://doi.org/10.1111/febs.13659 - Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase
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- Molecular recognition by CDC25B phosphatases
- Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation−π contacts in proteins
- Combining NMR and computer simulations to evaluate Cdc25B protein flexbility
- Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases
- Ligand binding and conformational dynamics of CDC25B phosphatase
- Expression, purification and buffering conditions of Cdc25B for NMR data acquisition
- Thermostability and protein structural networks: the role of hub residues
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