title: Refolding studies using pressure: the folding landscape of lysozyme in the pressure-temperature plane.
abstract: Refolding of hen egg white lysozyme after pressure unfolding was measured by FTIR spectroscopy. The high-pressure treatment was found to be useful for unfolding/refolding studies because pressure acts against aggregation, and therefore no irreversible aggregation takes place during the pressure treatment. After the release of the pressure, folding intermediate structures were found which were formed during the decompression of the lysozyme. These were aggregation prone when heated, as indicated by their lower stability against aggregation. The intermediates were only formed if the protein was unfolded, subdenaturing pressures could not populate these intermediates. We introduced the notion of a superfunnel to describe the free energy landscape of interacting polypeptide chains. This can explain the propensity of folding intermediates to aggregate. A possible Gibbs-free energy landscape for lysozyme was constructed for the whole pressure-temperature plane.
authors.affiliation: Department of Biophysics and Radiation Biology, Semmelweis University, Puskin u. 9, PF 263, H-1444 Budapest, Hungary. smeller@puskin.sote.hu
authors.forename: L
authors.initials: L
authors.lastname: Smeller
authors.forename: F
authors.initials: F
authors.lastname: Meersman
authors.forename: K
authors.initials: K
authors.lastname: Heremans
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D009113:Muramidase / Q000737:chemistry*; D011312:Pressure; D011485:Protein Binding; D011487:Protein Conformation; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
chemical_list: C421864:hen egg lysozyme; D009113:Muramidase