Structure-energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state.
نویسندگان
چکیده
We use infrared spectroscopy to study the evolution of protein folding intermediate structures on arbitrarily slow time scales by rapidly quenching thermally unfolded hen egg white lysozyme in a glassy matrix, followed by reheating of the protein to refold; upon comparison with differential scanning calorimetric experiments, low-temperature structural changes that precede the formation of energetic native contacts are revealed.
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ورودعنوان ژورنال:
- Chemical communications
دوره 29 شماره
صفحات -
تاریخ انتشار 2009