The role of calcium in the conformational dynamics and thermal stability of the D-galactose/D-glucose-binding protein from Escherichia coli

2005 ◽  
Vol 61 (1) ◽  
pp. 184-195 ◽  
Author(s):  
Petr Herman ◽  
Jaroslav Vecer ◽  
Ivan Barvik ◽  
Viviana Scognamiglio ◽  
Maria Staiano ◽  
...  
2005 ◽  
Vol 62 (1) ◽  
pp. 193-201 ◽  
Author(s):  
Anna Marabotti ◽  
Petr Herman ◽  
Maria Staiano ◽  
Antonio Varriale ◽  
Marcella de Champdoré ◽  
...  

2008 ◽  
Vol 20 (1) ◽  
pp. 330-337 ◽  
Author(s):  
Sabato d'Auria ◽  
Fabrizio Alfieri ◽  
Maria Staiano ◽  
Fabrizio Pelella ◽  
Mose' Rossi ◽  
...  

Sensors ◽  
2007 ◽  
Vol 7 (10) ◽  
pp. 2484-2491 ◽  
Author(s):  
Viviana Scognamiglio ◽  
Vincenzo Aurilia ◽  
Nunzio Cennamo ◽  
Paola Ringhieri ◽  
Luisa Iozzino ◽  
...  

2010 ◽  
Vol 24 (3-4) ◽  
pp. 355-359 ◽  
Author(s):  
Olga V. Stepanenko ◽  
Olga I. Povarova ◽  
Olesya V. Stepanenko ◽  
Alexander V. Fonin ◽  
Irina M. Kuznetsova ◽  
...  

The effects of guanidine hydrochloride (GdnHCl) on the structure and stability of the D-galactose/D-glucose-binding protein fromEscherichia coli(GGBP) and its complex with D-glucose (GGBP/Glc) were investigated by intrinsic protein fluorescence and far-UV circular dichroism (CD). The role of calcium in the stability of the protein structure was also studied. It was shown that the processes of GGBP and GGBP/Glc unfolding induced by GdnHCl followed one-step reversible denaturation mechanism. The obtained data showed that the binding of glucose to GGBP resulted in an increase of the protein stability towards the actions of the GdnHCl which made protein unfolding more cooperative. The stabilities of GGBP alone, GGBP in the presence of glucose, GGBP-depleted calcium (GGBP-Ca), and GGBP/Glc-depleted calcium (GGBP/Glc-Ca) were characterized by difference of Gibbs free energies.


2021 ◽  
Vol 46 (5) ◽  
pp. 4137-4153
Author(s):  
Neha Verma ◽  
Rob Delhez ◽  
Niek M. van der Pers ◽  
Frans D. Tichelaar ◽  
Amarante J. Böttger

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