engleski

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

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

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

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