Please use this identifier to cite or link to this item: http://repositorio.ufla.br/jspui/handle/1/28495
metadata.artigo.dc.title: Hydrophobic noncovalent interactions of inosine-phenylalanine: a theoretical model for investigating the molecular recognition of nucleobases
metadata.artigo.dc.creator: Santos, Lucas A.
Cunha, Elaine F. F. da
Freitas, Matheus P.
Ramalho, Teodorico C.
metadata.artigo.dc.subject: Molecular recognition process
Computational chemistry
Hydrophobic interactions
Processo de reconhecimento molecular
Química computacional
Interações hidrofóbicas
metadata.artigo.dc.publisher: American Chemical Society
metadata.artigo.dc.date.issued: 2014
metadata.artigo.dc.identifier.citation: SANTOS, L. A. et al. Hydrophobic noncovalent interactions of inosine-phenylalanine: a theoretical model for investigating the molecular recognition of nucleobases. The Journal of Physical Chemistry A, Washington, v. 118, n. 31, p. 5808-5817, 2014.
metadata.artigo.dc.description.abstract: Understanding the molecular recognition process of nucleobases is one of the greatest challenges for both computational chemistry and biophysics fields. In fact, our results point out that it is a hard task to take into account the hydrophobic interactions, such as π–π and T-stacking interactions, by theoretical calculations using conventional force fields due to quantum effects of hyperconjugation and electronic correlation. In this line, our findings put in evidence that simple modifications in the Lennard-Jones potential can improve theoretical predictions in scenarios where hydrophobic interactions can drive the molecular recognition.
metadata.artigo.dc.identifier.uri: http://pubs.acs.org/doi/abs/10.1021/jp411230w
http://repositorio.ufla.br/jspui/handle/1/28495
metadata.artigo.dc.language: en_US
Appears in Collections:DQI - Artigos publicados em periódicos

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