Single molecule FRET investigation of pressure-driven unfolding of cold shock protein A

2018 ◽  
Vol 148 (12) ◽  
pp. 123336 ◽  
Author(s):  
Sven Schneider ◽  
Hauke Paulsen ◽  
Kim Colin Reiter ◽  
Erik Hinze ◽  
Cordelia Schiene-Fischer ◽  
...  
Keyword(s):  
Single Molecule ◽  
Cold Shock ◽  
Protein A ◽  
Cold Shock Protein ◽  
Single Molecule Fret ◽  
Pressure Driven

Expression, purification and characterization of cold shock protein A of Corynebacterium pseudotuberculosis

2015 ◽  
Vol 112 ◽  
pp. 15-20 ◽  
Author(s):  
Antje Lindae ◽  
Raphael J. Eberle ◽  
Icaro P. Caruso ◽  
Monika A. Coronado ◽  
Fabio R. de Moraes ◽  
...  
Keyword(s):  
Cold Shock ◽  
Protein A ◽  
Cold Shock Protein ◽  
Corynebacterium Pseudotuberculosis ◽  
Purification And Characterization

Dynamical properties of cold shock protein A from Mycobacterium tuberculosis

2010 ◽  
Vol 402 (4) ◽  
pp. 693-698 ◽  
Author(s):  
Gabriella D’Auria ◽  
Carla Esposito ◽  
Lucia Falcigno ◽  
Luisa Calvanese ◽  
Emanuela Iaccarino ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Cold Shock ◽  
Protein A ◽  
Cold Shock Protein ◽  
Dynamical Properties

scholarly journals Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Haiyan Hong ◽  
Zilong Guo ◽  
Hao Sun ◽  
Ping Yu ◽  
Huanhuan Su ◽  
...  
Keyword(s):  
Single Molecule ◽  
Intermediate State ◽  
Cold Shock ◽  
Magnetic Tweezers ◽  
Single Step ◽  
Cold Shock Protein ◽  
Model Protein ◽  
Force Range ◽  
Step Over ◽  
Transient Intermediate

AbstractCold shock protein (Csp) is a typical two-state folding model protein which has been widely studied by biochemistry and single molecule techniques. Recently two-state property of Csp was confirmed by atomic force microscopy (AFM) through direct pulling measurement, while several long-lifetime intermediate states were found by force-clamp AFM. We systematically studied force-dependent folding and unfolding dynamics of Csp using magnetic tweezers with intrinsic constant force capability. Here we report that Csp mostly folds and unfolds with a single step over force range from 5 pN to 50 pN, and the unfolding rates show different force sensitivities at forces below and above ~8 pN, which determines a free energy landscape with two barriers and a transient intermediate state between them along one transition pathway. Our results provide a new insight on protein folding mechanism of two-state proteins.

Overexpression of Cold Shock Protein A of Psychromonas arctica KOPRI 22215 Confers Cold-Resistance

2010 ◽  
Vol 29 (2) ◽  
pp. 136-142 ◽  
Author(s):  
Youn Hong Jung ◽  
Ji-Yeun Yi ◽  
Hyun Jung Jung ◽  
Yoo Kyung Lee ◽  
Hong Kum Lee ◽  
...  
Keyword(s):  
Cold Shock ◽  
Cold Resistance ◽  
Protein A ◽  
Cold Shock Protein

scholarly journals Free energy landscape with two barriers and a transient intermediate state determining the unfolding and folding dynamics of cold shock protein

2021 ◽  
Author(s):  
Haiyan Hong ◽  
Zilong Guo ◽  
Hao Sun ◽  
Ping Yu ◽  
Huanhuan Su ◽  
...  
Keyword(s):  
Free Energy ◽  
Single Molecule ◽  
Cold Shock ◽  
Energy Landscape ◽  
Magnetic Tweezers ◽  
Single Step ◽  
Cold Shock Protein ◽  
Free Energy Landscape ◽  
Transient Intermediate ◽  
Two Barriers

Abstract Cold shock protein (Csp) is a typical two-state folding model protein which has been widely studied by biochemistry and single molecule techniques. Recently two-state property of Csp was confirmed by atomic force microscopy (AFM) through direct pulling measurement, while several long-lifetime intermediate states were found by force-clamp AFM. We systematically studied force-dependent folding and unfolding dynamics of Csp using magnetic tweezers with intrinsic constant force capability. We found that Csp mostly folds and unfolds with a single step over force range from 5 pN to 50 pN, and the unfolding rates show different force sensitivities at forces below and above ~ 8 pN, which determines a free energy landscape with two barriers and a transient intermediate between them along one transition pathway. Our results provide a new insight on protein folding mechanism of two-state proteins.

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