PMID:14517978

Citation	Salopek-Sondi, B, Skeels, MC, Swartz, D and Luck, LA (2003) Insight into the stability of the hydrophobic binding proteins of Escherichia coli: assessing the proteins for use as biosensors. Proteins 53:273-81
Abstract	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 LIV protein. A disulfide bond present in N-domain of both proteins makes a large contribution to the protein stability of these periplasmic binding receptors.
Links	PubMed Online version:10.1002/prot.10485
Keywords	Bacterial Proteins; Biosensing Techniques; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Hydrophobic and Hydrophilic Interactions; Ligands; Models, Molecular; Protein Denaturation; Protein Folding; Receptors, Amino Acid/chemistry; Receptors, Amino Acid/metabolism
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.