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Autori: S. Cavalu, S. Cinta Pinzaru, N. Leopold, W. Kiefer
Editorial: Elsevier, Biopolimers/Biospectroscopy, 62, p.341-348, 2001.
Tempyo labelled bovine serum albumin and cytochrome c at different pH values were prepared and investigated using Raman/resonance Raman and SERS spectroscopy. Raman spectra of tempyo labelled proteins in the pH range from 6.7 to 11 were compared to those of the corresponding free species. SERS spectra were interpreted in terms of adsorption-induced structural changes of tempyo labelled proteins on the silver colloidal surface. Tempyo spin label was found to be inactive in the Raman/resonance Raman and SERS spectra of proteins. As the SERS binding site of bovine serum albumin a-helix conformation was concluded to be more favourable. In the case of cytochrome c, the enhancement of the bands assigned to porphyrine macrocycle stretching mode allowed the supposition of N-adsorption to the colloidal surface.
Cuvinte cheie: tempyo labelled proteines, Raman, SERS