Chem. J. Chinese Universities

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Heat-Induced Changes of Secondary Structures of BSA in D2O Studied by Infrared Spectroscopy and Window Factor Analysis

YUAN Bo*, YAN Hui-Min   

  1. State Key Laboratory of Modern Optical Instrumentation, CNERC for Optical Instrument, Zhejiang University, Hangzhou 310027, China
  • Received:2007-07-02 Revised:1900-01-01 Online:2007-12-10 Published:2007-12-10
  • Contact: YUAN Bo

Abstract: Heat-induced changes of secondary structures of bovine serum albumin(BSA) in D2O was studied by using infrared spectroscopy and window factor analysis(WFA). The results obtained from the conventional spectral analysis methods and WFA indicate that conformational changes of BSA began at 56 ℃, while the drastic variations of secondary structures occurred in the temperature range of 68—82 ℃. Additionally, the temperature at which the variation of short-segment chains connecting α-helical segment took place is lower by round 10 ℃ than that of the other secondary structures. The present study reveals that WFA plays a key role in the analysis the temperature-dependent infrared spectra of protein in solution.

Key words: Infrared spectroscopy, Window factor analysis(WFA), Heating, Bovine serum albumin(BSA), Secondary structure

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