Articolo in rivista, 2022, ENG, 10.1016/j.bpj.2022.03.010
Puglisi Rita, Cioni Patrizia, Gabellieri Edi, Presciuttini Gianluca, Pastore Annalisa and Temussi Piero Andrea
Pastore, A (Corresponding Author), Kings Coll London, UK DRI Wohl Inst, London, England. Pastore, A (Corresponding Author), European Synchrotron Radiat Facil, Grenoble, France. Puglisi, Rita; Pastore, Annalisa; Temussi, Piero Andrea, Kings Coll London, UK DRI Wohl Inst, London, England. Cioni, Patrizia; Gabellieri, Edi; Presciuttini, Gianluca, CNR, Ist Biofis, Pisa, Italy. Pastore, Annalisa, European Synchrotron Radiat Facil, Grenoble, France.
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 degrees 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.
Biophysical journal (Print) 121 (8), pp. 1502–1511
FREE-ENERGY-LANDSCAPE, PROTEIN DENATURATION, STAPHYLOCOCCAL NUCLEASE, THERMAL-STABILITY, VOLUME CHANGE, IRON-BINDING, TEMPERATURE, HYDRATION, NMR, PHOSPHORESCENCE
Gabellieri Edi, Presciuttini Gianluca, Cioni Patrizia
ID: 472732
Year: 2022
Type: Articolo in rivista
Creation: 2022-11-04 08:46:32.000
Last update: 2022-11-29 11:47:29.000
CNR institutes
External IDs
CNR OAI-PMH: oai:it.cnr:prodotti:472732
DOI: 10.1016/j.bpj.2022.03.010
ISI Web of Science (WOS): 000793038200014