Structure-energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state.
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.
Cho
Theresa Y
TY
Department of Chemical Engineering, Princeton University, Princeton, NJ 08544, USA.
Byrne
Nolene
N
Moore
David J
DJ
Pethica
Brian A
BA
Angell
C Austen
CA
Debenedetti
Pablo G
PG
D000818:Animals; D002152:Calorimetry, Differential Scanning; D002645:Chickens; D007259:Infrared Rays; D009113:Muramidase / Q000737:chemistry*; D017510:Protein Folding
C421864:hen egg lysozyme; D009113:Muramidase