TY  - JOUR
AU  - Minić, Simeon L.
AU  - Annighofer, Burkhard
AU  - Helary, Arnaud
AU  - Sago, Laıla
AU  - Cornu, David
AU  - Brulet, Annie
AU  - Combet, Sophie
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5690
AB  - High pressure (HP) is a particularly powerful tool to study protein folding/unfolding, revealing subtle structural rearrangements.
Bovine b-lactoglobulin (BLG), a protein of interest in food science, exhibits a strong propensity to bind various
bioactive molecules. We probed the effects of the binding of biliverdin (BV), a tetrapyrrole linear chromophore, on the stability
of BLG under pressure, by combining in situ HP small-angle neutron scattering (SANS) and HP-UV absorption spectroscopy.
Although BV induces a slight destabilization of BLG during HP-induced unfolding, a ligand excess strongly prevents BLG oligomerization.
Moreover, at SANS resolution, an excess of BV induces the complete recovery of the protein ‘‘native’’ 3D structure
after HP removal, despite the presence of the BV covalently bound adduct. Mass spectrometry highlights the crucial role of
cysteine residues in the competitive and protective effects of BV during pressure denaturation of BLG through SH/S-S
exchange.
PB  - Biophysical Society
T2  - Biophysical Journal
T1  - Structure of proteins under pressure: Covalent binding effects of biliverdin on b-lactoglobulin
VL  - 121
SP  - 1
EP  - 12
DO  - 10.1016/j.bpj.2022.06.003
ER  - 

@article{
author = "Minić, Simeon L. and Annighofer, Burkhard and Helary, Arnaud and Sago, Laıla and Cornu, David and Brulet, Annie and Combet, Sophie",
year = "2022",
abstract = "High pressure (HP) is a particularly powerful tool to study protein folding/unfolding, revealing subtle structural rearrangements.
Bovine b-lactoglobulin (BLG), a protein of interest in food science, exhibits a strong propensity to bind various
bioactive molecules. We probed the effects of the binding of biliverdin (BV), a tetrapyrrole linear chromophore, on the stability
of BLG under pressure, by combining in situ HP small-angle neutron scattering (SANS) and HP-UV absorption spectroscopy.
Although BV induces a slight destabilization of BLG during HP-induced unfolding, a ligand excess strongly prevents BLG oligomerization.
Moreover, at SANS resolution, an excess of BV induces the complete recovery of the protein ‘‘native’’ 3D structure
after HP removal, despite the presence of the BV covalently bound adduct. Mass spectrometry highlights the crucial role of
cysteine residues in the competitive and protective effects of BV during pressure denaturation of BLG through SH/S-S
exchange.",
publisher = "Biophysical Society",
journal = "Biophysical Journal",
title = "Structure of proteins under pressure: Covalent binding effects of biliverdin on b-lactoglobulin",
volume = "121",
pages = "1-12",
doi = "10.1016/j.bpj.2022.06.003"
}

Minić, S. L., Annighofer, B., Helary, A., Sago, L., Cornu, D., Brulet, A.,& Combet, S.. (2022). Structure of proteins under pressure: Covalent binding effects of biliverdin on b-lactoglobulin. in Biophysical Journal
Biophysical Society., 121, 1-12.
https://doi.org/10.1016/j.bpj.2022.06.003

Minić SL, Annighofer B, Helary A, Sago L, Cornu D, Brulet A, Combet S. Structure of proteins under pressure: Covalent binding effects of biliverdin on b-lactoglobulin. in Biophysical Journal. 2022;121:1-12.
doi:10.1016/j.bpj.2022.06.003 .

Minić, Simeon L., Annighofer, Burkhard, Helary, Arnaud, Sago, Laıla, Cornu, David, Brulet, Annie, Combet, Sophie, "Structure of proteins under pressure: Covalent binding effects of biliverdin on b-lactoglobulin" in Biophysical Journal, 121 (2022):1-12,
https://doi.org/10.1016/j.bpj.2022.06.003 . .