Title: High pressure induces the formatim of aggregation-prone states of proteins under reducing conditions
Authors: Meersman, Filip ×
Heremans, Karel #
Issue Date: Jan-2003
Publisher: Elsevier science bv
Series Title: Biophysical chemistry vol:104 issue:1 pages:297-304
Abstract: The pressure stability of ribonuclease A and bovine pancreatic trypsin inhibitor has been investigated with Fourier transform infrared spectroscopy in the presence of the disulfide bond reducing agent 2-mercaptoethanol. The secondary structure of the reduced proteins at high pressure (1 GPa) is not significantly different from the pressure-induced conformation of the native form. Upon decompression under reducing conditions, amorphous aggregates are formed. Such aggregates are not formed upon decompression of the native proteins. Our, data demonstrate that high pressure populates, and thus allows the potential characterization of highly aggregation-prone conformations. The relevance of these findings with regard to fibril formation is discussed and the possible role of conformational fluctuations of intermediates on the aggregation pathway is emphasized. (C) 2003 Elsevier Science B.V. All-rights reserved.
ISSN: 0301-4622
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

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