Abstract
a-helix, þ-sheet, þ-turns, and random coils are the three-dimensional local segments that constitute a protein secondary structure. Molecular vibrations of proteins are sensitive to structural organizations of peptide chains hence Fourier Transform infrared (FTIR) spectroscopy is one of the recognized techniques for the identification of protein secondary structures. However, the lower frequency region of FTIR especially the amide VI bands (in the region 590-490cm-1) is little studied for proteins. Further, the effect of sugar-free natura on ovalbumin stability is not yet studied to our knowledge. The present study examines the conformational changes in the secondary structure of ovalbumin (OVA) protein under the influence of pH variations (2, 5, 7, 9, and 12) and also cosolvent sugar-free Natura (SFN) inclusion. From the primary absorption spectra of the amide VI bands, the second derivative analysis is furnished to quantify the secondary structural elements of protein thereby conformational changes are analyzed. From obtained results, it is found that conformational changes occur between two major secondary structures of a-helix and þ-sheet of OVA due to variation of pH and inclusion of cosolvent. Also, the results confirm that the denaturation of OVA in the presence of SFN irrespective of pH.
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