OSA's Digital Library

Applied Spectroscopy

Applied Spectroscopy


  • Vol. 61, Iss. 9 — Sep. 1, 2007
  • pp: 921–927

Study of Thermal Dynamics of Defatted Bovine Serum Albumin in D2O Solution by Fourier Transform Infrared Spectra and Evolving Factor Analysis

Bo Yuan, Koichi Murayama, and Huiming Yan

Applied Spectroscopy, Vol. 61, Issue 9, pp. 921-927 (2007)

View Full Text Article

Acrobat PDF (206 KB)

Browse Journals / Lookup Meetings

Browse by Journal and Year


Lookup Conference Papers

Close Browse Journals / Lookup Meetings

Article Tools

  • Export Citation/Save Click for help


Fourier transform infrared (FT-IR) spectra have been measured for defatted bovine serum albumin (BSA) in D<sub>2</sub>O with a concentration of 2.0 wt % over a temperature range of 26–90 °C and the corresponding difference spectra have been calculated by subtracting the contribution of D<sub>2</sub>O at the same temperature. Evolving factor analysis (EFA) by selecting two factors and three factors has been employed to analyze the temperature-dependent difference IR spectra in the 1700–1600 cm<sup>–1</sup> spectral region of the defatted BSA in D<sub>2</sub>O solution. Three-factor EFA has been employed to determine the distinction of the three protein species involved in the process of temperature elevation: native, transitional, and denatured protein. The temperature profiles obtained from three-factor EFA indicate that heat-induced conformational change in the secondary structures of defatted BSA in D<sub>2</sub>O undergoes two two-state transitions, a drastic transition and a slight transition, which occur in the temperature ranges of 68–82 °C and 56–76 °C, respectively.

Virtual Issues
Vol. 2, Iss. 10 Virtual Journal for Biomedical Optics

Bo Yuan, Koichi Murayama, and Huiming Yan, "Study of Thermal Dynamics of Defatted Bovine Serum Albumin in D2O Solution by Fourier Transform Infrared Spectra and Evolving Factor Analysis," Appl. Spectrosc. 61, 921-927 (2007)

Sort:  Journal  |  Reset


References are not available for this paper.

Cited By

OSA is able to provide readers links to articles that cite this paper by participating in CrossRef's Cited-By Linking service. CrossRef includes content from more than 3000 publishers and societies. In addition to listing OSA journal articles that cite this paper, citing articles from other participating publishers will also be listed.

« Previous Article  |  Next Article »

OSA is a member of CrossRef.

CrossCheck Deposited