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Author Griebenow, K.; Klibanov, A.M. url  doi
  Title (up) Lyophilization-induced reversible changes in the secondary structure of proteins Type Journal Article
  Year 1995 Publication Proc Natl Acad Sci USA Abbreviated Journal  
  Volume 92 Issue 24 Pages 10969-10976  
  Abstract Changes in the secondary structure of some dozen different proteins upon lyophilization of their aqueous solutions have been investigated by means of Fourier-transform infrared spectroscopy in the amide III band region. Dehydration markedly (but reversibly) alters the secondary structure of all the proteins studied, as revealed by both the quantitative analysis of the second derivative spectra and the Gaussian curve fitting of the original infrared spectra. Lyophilization substantially increases the beta-sheet content and lowers the alpha-helix content of all proteins. In all but one case, proteins become more ordered upon lyophilization.  
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  Call Number Equine Behaviour @ team @ Serial 6519  
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