Title: Pressure stability of insulin: A Fourier transform infrared spectroscopy study
Authors: Dirix, Carolien ×
Meersman, Filip
Heremans, Karel #
Issue Date: Jan-2003
Publisher: Taylor & francis ltd
Series Title: High pressure research vol:23 issue:1-2 pages:63-66
Abstract: High hydrostatic pressure can induce partially unfolded protein conformations that are highly aggregation prone under conditions that normally favour the native state. We investigated the pressure stability of insulin at pH 2 with Fourier transform infrared spectroscopy. We do not observe any cooperative change up to 13 kbar. All spectral changes in the amide I area are fully reversible and are assumed to arise from the elastic effect of pressure, which causes no conformational changes. Moreover, insulin has no higher temperature-induced aggregation tendency when pressure pre-treated.
ISSN: 0895-7959
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Chemistry - miscellaneous
Molecular Imaging and Photonics
Biochemistry, Molecular and Structural Biology Section
× corresponding author
# (joint) last author

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