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Heat and cold denaturation of yeast frataxin: The effect of pressure

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Heat and cold denaturation of yeast frataxin : The effect of pressure. / Puglisi, Rita; Cioni, Patrizia; Gabellieri, Edi et al.

In: Biophysical Journal, Vol. 121, No. 8, 19.04.2022, p. 1502-1511.

Research output: Contribution to journalArticlepeer-review

Harvard

Puglisi, R, Cioni, P, Gabellieri, E, Presciuttini, G, Pastore, A & Temussi, PA 2022, 'Heat and cold denaturation of yeast frataxin: The effect of pressure', Biophysical Journal, vol. 121, no. 8, pp. 1502-1511. https://doi.org/10.1016/j.bpj.2022.03.010

APA

Puglisi, R., Cioni, P., Gabellieri, E., Presciuttini, G., Pastore, A., & Temussi, P. A. (2022). Heat and cold denaturation of yeast frataxin: The effect of pressure. Biophysical Journal, 121(8), 1502-1511. https://doi.org/10.1016/j.bpj.2022.03.010

Vancouver

Puglisi R, Cioni P, Gabellieri E, Presciuttini G, Pastore A, Temussi PA. Heat and cold denaturation of yeast frataxin: The effect of pressure. Biophysical Journal. 2022 Apr 19;121(8):1502-1511. https://doi.org/10.1016/j.bpj.2022.03.010

Author

Puglisi, Rita ; Cioni, Patrizia ; Gabellieri, Edi et al. / Heat and cold denaturation of yeast frataxin : The effect of pressure. In: Biophysical Journal. 2022 ; Vol. 121, No. 8. pp. 1502-1511.

Bibtex Download

@article{23569b040cca4d7496690b646a5f55a5,
title = "Heat and cold denaturation of yeast frataxin: The effect of pressure",
abstract = "Yfh1 is a yeast protein with the peculiar characteristic to undergo, in the absence of salt, cold denaturation at temperatures above the water freezing point. This feature makes the protein particularly interesting for studies aiming at understanding the rules that determine protein fold stability. Here, we present the phase diagram of Yfh1 unfolding as a function of pressure (0.1–500 MPa) and temperature 278–313 K (5–40°C) both in the absence and in the presence of stabilizers using Trp fluorescence as a monitor. The protein showed a remarkable sensitivity to pressure: at 293 K, pressures around 10 MPa are sufficient to cause 50% of unfolding. Higher pressures were required for the unfolding of the protein in the presence of stabilizers. The phase diagram on the pressure-temperature plane together with a critical comparison between our results and those found in the literature allowed us to draw conclusions on the mechanism of the unfolding process under different environmental conditions.",
author = "Rita Puglisi and Patrizia Cioni and Edi Gabellieri and Gianluca Presciuttini and Annalisa Pastore and Temussi, {Piero Andrea}",
note = "Funding Information: The work was funded by the Dementia Research Institute (grant Nr RE1 3556 ), which is funded by the Medical Research Council , Alzheimer{\textquoteright}s Society, and Alzheimer{\textquoteright}s Research UK. Publisher Copyright: {\textcopyright} 2022 Biophysical Society",
year = "2022",
month = apr,
day = "19",
doi = "10.1016/j.bpj.2022.03.010",
language = "English",
volume = "121",
pages = "1502--1511",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Elsevier BV",
number = "8",

}

RIS (suitable for import to EndNote) Download

TY - JOUR

T1 - Heat and cold denaturation of yeast frataxin

T2 - The effect of pressure

AU - Puglisi, Rita

AU - Cioni, Patrizia

AU - Gabellieri, Edi

AU - Presciuttini, Gianluca

AU - Pastore, Annalisa

AU - Temussi, Piero Andrea

N1 - Funding Information: The work was funded by the Dementia Research Institute (grant Nr RE1 3556 ), which is funded by the Medical Research Council , Alzheimer’s Society, and Alzheimer’s Research UK. Publisher Copyright: © 2022 Biophysical Society

PY - 2022/4/19

Y1 - 2022/4/19

N2 - Yfh1 is a yeast protein with the peculiar characteristic to undergo, in the absence of salt, cold denaturation at temperatures above the water freezing point. This feature makes the protein particularly interesting for studies aiming at understanding the rules that determine protein fold stability. Here, we present the phase diagram of Yfh1 unfolding as a function of pressure (0.1–500 MPa) and temperature 278–313 K (5–40°C) both in the absence and in the presence of stabilizers using Trp fluorescence as a monitor. The protein showed a remarkable sensitivity to pressure: at 293 K, pressures around 10 MPa are sufficient to cause 50% of unfolding. Higher pressures were required for the unfolding of the protein in the presence of stabilizers. The phase diagram on the pressure-temperature plane together with a critical comparison between our results and those found in the literature allowed us to draw conclusions on the mechanism of the unfolding process under different environmental conditions.

AB - Yfh1 is a yeast protein with the peculiar characteristic to undergo, in the absence of salt, cold denaturation at temperatures above the water freezing point. This feature makes the protein particularly interesting for studies aiming at understanding the rules that determine protein fold stability. Here, we present the phase diagram of Yfh1 unfolding as a function of pressure (0.1–500 MPa) and temperature 278–313 K (5–40°C) both in the absence and in the presence of stabilizers using Trp fluorescence as a monitor. The protein showed a remarkable sensitivity to pressure: at 293 K, pressures around 10 MPa are sufficient to cause 50% of unfolding. Higher pressures were required for the unfolding of the protein in the presence of stabilizers. The phase diagram on the pressure-temperature plane together with a critical comparison between our results and those found in the literature allowed us to draw conclusions on the mechanism of the unfolding process under different environmental conditions.

UR - http://www.scopus.com/inward/record.url?scp=85127608442&partnerID=8YFLogxK

U2 - 10.1016/j.bpj.2022.03.010

DO - 10.1016/j.bpj.2022.03.010

M3 - Article

VL - 121

SP - 1502

EP - 1511

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 8

ER -

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