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1.
Phys Chem Chem Phys ; 17(18): 12207-14, 2015 May 14.
Artigo em Inglês | MEDLINE | ID: mdl-25892296

RESUMO

Temperature-dependent Raman and dielectric measurements have been carried out on (C2H5NH3)2CdCl4 single crystals. Raman studies reveal the presence of two structural phase transitions below room temperature at 216 K and 114 K. The phase transitions are marked by anomalies in temperature dependence of wave-number and full width half maximum (FWHM) of several vibrational modes. The transitions are also accompanied by anomalies in dielectric measurements. Raman and dielectric data indicate that the transition at 216 K is order-disorder in nature and is driven by re-orientation of organic ions, while the transition at 114 K is due to coupling between the CdCl6 octahedron and the organic chain. Further high temperature dielectric measurements reveal the presence of one more structural phase transition around 473 K across which dispersion in dielectric parameters is observed. The activation energies and relaxation time obtained for high temperature dielectric phases are characteristic of combined reorientation motions of alkyl ammonium cations.

2.
J Phys Chem B ; 118(20): 5322-30, 2014 May 22.
Artigo em Inglês | MEDLINE | ID: mdl-24783979

RESUMO

We demonstrate the utility of the surface-enhanced Raman spectroscopy (SERS) to monitor conformational transitions in protein upon ligand binding. The changes in protein's secondary and tertiary structures were monitored using amide and aliphatic/aromatic side chain vibrations. Changes in these bands are suggestive of the stabilization of the secondary and tertiary structure of transcription activator protein C in the presence of Mg(2+) ion, whereas the spectral fingerprint remained unaltered in the case of a mutant protein, defective in Mg(2+) binding. The importance of the acidic residues in Mg(2+) binding, which triggers an overall allosteric transition in the protein, is visualized in the molecular model. The present study thus opens up avenues toward the application of SERS as a potential tool for gaining structural insights into the changes occurring during conformational transitions in proteins.


Assuntos
Magnésio/química , Análise Espectral Raman , Transativadores/química , Regulação Alostérica , Sítios de Ligação , Coloides/química , Íons/química , Simulação de Dinâmica Molecular , Mutação , Estrutura Secundária de Proteína , Estrutura Terciária de Proteína , Prata/química , Transativadores/genética , Transativadores/metabolismo
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