G. DAMIAN, V. CÂNPEAN

Dept. of Biomedical Physics, Physics Faculty, “Babeş-Bolyai” University, 1A, Kogălniceanu, 400084-Cluj-Napoca, Romania

Abstract. The conformational changes of bovine hemoglobin at different pH values have been studied by FT-IR spectrometry using an Attenuated Total Reflectance (ATR) accessory. Changes in the amide bands in Fourier transform infrared spectra of proteins are generally attributed to alterations in protein secondary structure. In this study the spectra of hemoglobin at different pH values were analyzed. The second-derivative analysis of infrared spectra permits direct quantitative analysis of the secondary structural components of proteins by integration and curve fitting

Corresponding author’s e-mail: dgrig@phys.ubbcluj.ro

Full text: PDF