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