Janet Olchowicz, Deidra R. Coles, Lori E. Kain, Gina MacDonald
This report describes a laboratory that employs infrared spectroscopy to observe protein secondary structure. The techniques utilized are suitable for all levels of biochemistry or biophysical chemistry laboratories. Students first obtain absorbance spectra on proteins that are predominately composed of either α helixes or β sheets in order to understand how infrared is used to study secondary structure. For an extended laboratory we describe how infrared spectroscopy can be used to monitor the unfolding of myoglobin. The same techniques could easily be applied to any protein or to monitor the unfolding of any predominately α-helical protein whose characterization is of interest.
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