Title: Refolding studies using pressure: The folding landscape of lysozyme in the pressure-temperature plane
Authors: Smeller, L ×
Meersman, Filip
Heremans, Karel #
Issue Date: Jan-2006
Publisher: Elsevier science bv
Series Title: Biochimica et biophysica acta-proteins and proteomics vol:1764 issue:3 pages:497-505
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-ftee energy landscape for lysozyme was constructed for the whole pressure-temperature plane. (c) 2006 Elsevier B.V. All rights reserved.
ISSN: 1570-9639
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Imaging and Photonics
Biochemistry, Molecular and Structural Biology Section
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science