Pick and Choose the Spectroscopic Method to Calibrate the Local Electric Field inside Proteins.
J Phys Chem Lett
; 7(13): 2456-60, 2016 Jul 07.
Article
em En
| MEDLINE
| ID: mdl-27295386
ABSTRACT
Electrostatic interactions in proteins play a crucial role in determining the structure-function relation in biomolecules. In recent years, fluorescent probes have been extensively employed to interrogate the polarity in biological cavities through dielectric constants or semiempirical polarity scales. A choice of multiple spectroscopic methods, not limited by fluorophores, along with a molecular level description of electrostatics involving solute-solvent interactions, would allow more flexibility to pick and choose the experimental technique to determine the local electrostatics within protein interiors. In this work we report that ultraviolet/visible-absorption, infrared-absorption, or (13)C NMR can be used to calibrate the local electric field in both hydrogen bonded and non-hydrogen bonded protein environments. The local electric field at the binding site of a serum protein has been determined using the absorption wavelength as well as the carbonyl stretching frequency of its natural steroid substrate, testosterone. Excellent agreement is observed in the results obtained from two independent spectroscopic techniques.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Espectroscopia de Ressonância Magnética
/
Proteínas
/
Eletricidade Estática
/
Ligação de Hidrogênio
Idioma:
En
Revista:
J Phys Chem Lett
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Índia