Background: Stefin B, an established model protein for studying the
stability and mechanism of protein folding, was used for monitoring protein
aggregation and formation of amyloid structure by infrared spectroscopy.
Methods: The analyses of the integral intensities of the low frequency
part of the Amide I band, which is directly connected to the appearance of the
cross-
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Open Access
Original Research
Amyloid Formation of Stefin B Protein Studied by Infrared Spectroscopy
Urban Novak1, Eva Žerovnik2, Ajda Taler-Verčič2, MagdaTušek Žnidarič3, Barbara Zupančič1, Jože Grdadolnik1,*
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1
Theory Department, National Institute of Chemistry, SI-1000 Ljubljana, Slovenia
2
Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute, SI-1000 Ljubljana, Slovenia
3
Department of Biotechnology and Systems Biology, National Institute of Biology, SI-1000 Ljubljana, Slovenia
*Correspondence: joze.grdadolnik@ki.si (Jože Grdadolnik)
Front. Biosci. (Landmark Ed) 2023, 28(3), 46;
https://doi.org/10.31083/j.fbl2803046
Submitted: 23 December 2022 | Revised: 1 February 2023 | Accepted: 23 February 2023 | Published: 6 March 2023
(This article belongs to the Special Issue Protein Folding, Design and Aggregation: New Aspects and Uses)
Copyright: © 2023 The Author(s). Published by IMR Press.
This is an open access article under the CC BY 4.0 license.
Abstract
Keywords
stefin B
amyloid formation
infrared spectroscopy
aggregation
structure analysis
Graphical Abstract
Funding
P1-0010/Slovenian Research Agency (ARRS), Slovenia
J1-1705/Slovenian Research Agency (ARRS), Slovenia
Figures
Fig. 1.