Naslov
Insight into the stability of the hydrophobic binding proteins of Escherichia coli: Assessing the proteins for use as biosensors

Autori
Salopek-Sondi, Branka ; Skeels, Matthew C. ; Swartz, Derrick ; Luck, Linda A.

Izvornik
Proteins: Structure, Function, and Genetics (0887-3585) 53 (2003); 273-281

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Protein unfolding; Escherichia coli; Leucine specific binding protein; Leucine-isoleucine-valine specific binding protein; Ligand-dependent conformational stability

Sažetak
Spectroscopic methods were used to monitor the unfolding of the leucine specific (LS) and the leucine-isoleucine-valine (LIV) binding proteins. Our studies indicate that ligand-free protein undergoes a simple two-state unfolding, whereas the protein-ligand complex undergoes a three-state unfolding model. Ligand binding causes significant stabilization of both proteins. There is correlation between ligand hydrophobicity and protein stabilization: The most hydrophobic ligand, isoleucine, causes the most significant stabilization of the LIV protein. A disulfide bond present in the N-domain of both proteins makes a large contribution to the protein stability of the periplasmic binding receptors

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA