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Fourier protein unfolding

Fourier transform infrared (FTIR) vibrational spectroscopy senses the hydrogen bonding pattern of the peptide bonds of a protein and can detect unfolding transitions in terms of changes in the secondary stmcture patterns. As compared to CD, which also senses secondary stmcture, FTIR is relatively more responsive to jS-sheet stmc-tures. A disadvantage of FTIR is that it requires a higher protein concentration and that it is more difficult to automate for titration experiments. [Pg.148]

See other pages where Fourier protein unfolding is mentioned: [Pg.690]    [Pg.173]    [Pg.93]    [Pg.272]    [Pg.155]    [Pg.176]    [Pg.6563]    [Pg.368]    [Pg.14]    [Pg.67]    [Pg.202]    [Pg.6562]    [Pg.329]    [Pg.340]    [Pg.327]   
See also in sourсe #XX -- [ Pg.2 , Pg.92 ]



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Protein unfolding

Unfolded

Unfolded proteins

Unfolders

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