Study of pK Values and Effective Dielectric Constants of Ionizable Residues in Pentapeptides and in Staphylococcal Nuclease (SNase) Using a Mean-Field Approach

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniv Jena
dc.creatorBossa, Guilherme Volpe [UNESP]
dc.creatorFahr, Alfred
dc.creatorSouza, Tereza Pereira de [UNESP]
dc.date2014-12-03T13:09:00Z
dc.date2014-12-03T13:09:00Z
dc.date2014-04-17
dc.date.accessioned2023-09-09T09:49:38Z
dc.date.available2023-09-09T09:49:38Z
dc.identifierhttp://dx.doi.org/10.1021/jp411331p
dc.identifierJournal Of Physical Chemistry B. Washington: Amer Chemical Soc, v. 118, n. 15, p. 4053-4061, 2014.
dc.identifier1520-6106
dc.identifierhttp://hdl.handle.net/11449/111823
dc.identifier10.1021/jp411331p
dc.identifierWOS:000334731300001
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8761482
dc.descriptionThe determination of pK values of amino acid residues as a function of temperature and ionic concentration is crucial to understanding the dynamics of various biological processes such as adsorption of peptides and their interactions with active sites of enzymes. In this study we developed a mean-field model to calculate the position-dependent dielectric constants of ionizable groups and the mean electrostatic potential on the surface. Such potential, which takes into account the contributions exerted by neighboring groups and ions in solution, is responsible for the fine-tuning of the pK value of each residue. The proposed model was applied to the amino acids Asp, Glu, Lys, His, Tyr, and Cys, and since the results were consistent with experimentally obtained values, the model was extended and applied to computation of pK values of Gly and Ala pentapeptides and of ionizable residues of the enzyme staphylococcal nuclease (SNase). In this latter case, we used an approach similar to a first-neighbors approximation, and the results turned out to be in good agreement with previously reported data when considering only the interactions of charged groups located at distances of maximally 20 angstrom. These considerations and the little computational cost involved turn the suggested approach into a promising tool for the modeling of force fields in computational simulations.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionAlexander von Humboldt Foundatio
dc.descriptionSao Paulo State Univ, Inst Biociencias Letras & Ciencias Exatas, BR-15054000 Sao Jose Do Rio Preto, Brazil
dc.descriptionUniv Jena, Inst Pharm, D-07743 Jena, Germany
dc.descriptionSao Paulo State Univ, Inst Biociencias Letras & Ciencias Exatas, BR-15054000 Sao Jose Do Rio Preto, Brazil
dc.descriptionFAPESP: 11/03150-8
dc.format4053-4061
dc.languageeng
dc.publisherAmer Chemical Soc
dc.relationJournal of Physical Chemistry B
dc.relation3.146
dc.relation1,331
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.titleStudy of pK Values and Effective Dielectric Constants of Ionizable Residues in Pentapeptides and in Staphylococcal Nuclease (SNase) Using a Mean-Field Approach
dc.typeArtigo


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