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Linear and Nonlinear Dielectric Response of Intrinsically Disordered Proteins.
Sauer, Michael A; Colburn, Taylor; Maiti, Sthitadhi; Heyden, Matthias; Matyushov, Dmitry V.
Afiliación
  • Sauer MA; School of Molecular Sciences, Arizona State University, PO Box 871504, Tempe, Arizona 85287-1504, United States.
  • Colburn T; Department of Physics, Arizona State University, PO Box 871504, Tempe, Arizona 85287-1504, United States.
  • Maiti S; School of Molecular Sciences, Arizona State University, PO Box 871504, Tempe, Arizona 85287-1504, United States.
  • Heyden M; School of Molecular Sciences, Arizona State University, PO Box 871504, Tempe, Arizona 85287-1504, United States.
  • Matyushov DV; School of Molecular Sciences and Department of Physics, Arizona State University, PO Box 871504, Tempe, Arizona 85287-1504, United States.
J Phys Chem Lett ; 15(20): 5420-5427, 2024 May 23.
Article en En | MEDLINE | ID: mdl-38743557
ABSTRACT
Linear and nonlinear dielectric responses of solutions of intrinsically disordered proteins (IDPs) were analyzed by combining molecular dynamics simulations with formal theories. A large increment of the linear dielectric function over that of the solvent is found and related to large dipole moments of IDPs. The nonlinear dielectric effect (NDE) of the IDP far exceeds that of the bulk electrolyte, offering a route to interrogate protein conformational and rotational statistics and dynamics. Conformational flexibility of the IDP makes the dipole moment statistics consistent with the gamma/log-normal distributions and contributes to the NDE through the dipole moment's non-Gaussian parameter. The intrinsic non-Gaussian parameter of the dipole moment combines with the protein osmotic compressibility in the nonlinear dielectric susceptibility when dipolar correlations are screened by the electrolyte. The NDE is dominated by dipolar correlations when electrolyte screening is reduced.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Simulación de Dinámica Molecular / Proteínas Intrínsecamente Desordenadas Idioma: En Revista: J Phys Chem Lett Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Simulación de Dinámica Molecular / Proteínas Intrínsecamente Desordenadas Idioma: En Revista: J Phys Chem Lett Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos