Publication
Title
Native state dynamics affects the folding transition of porcine pancreatic phospholipase
Author
Abstract
Porcine pancreatic phospholipase A(2), a small and disulfide rich protein, is extremely resistant against chemically or thermally induced unfolding. Despite this marked resistance, the protein displays broad unfolding transitions resulting in comparatively low apparent thermodynamic stability. Broad unfolding transitions may result from undetected folding intermediates, residual structures in the unfolded state or an inhomogeneity of the native state. Using circular dichroism, fluorescence, and NMR spectroscopy, we ruled out the existence of stably populated folding intermediates, whereas UV absorbance measurements hinted at stable residual structures in the unfolded state. These residual structures proved, however, to have no impact on the folding parameters. Studies by limited proteolysis, CD, and NMR spectroscopy under non-denaturing conditions suggested pronounced dynamics of the protein in the native state, which as long as unrestrained by acidic pH or bound Ca2+ ions exert considerable influence on the unfolding transition. (C) 2015 Elsevier B.V. All rights reserved.
Language
English
Source (journal)
Biophysical chemistry. - Amsterdam
Publication
Amsterdam : 2015
ISSN
0301-4622
Volume/pages
206(2015), p. 12-21
ISI
000361259000002
Full text (Publisher's DOI)
Full text (publisher's version - intranet only)
UAntwerpen
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identification
Creation 13.11.2015
Last edited 21.07.2017
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