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 m...

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Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2003-11, Vol.53 (2), p.273-281
Main Authors: Salopek-Sondi, Branka, Skeels, Matthew C., Swartz, Derrick, Luck, Linda A.
Format: Article
Language:English
Subjects:
Bacterial Proteins
Biosensing Techniques
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Hydrophobic and Hydrophilic Interactions
leucine- isoleucine-valine binding proteins
leucine-specific binding proteins
Ligands
Models, Molecular
Protein Denaturation
Protein Folding
proteins stability
Receptors, Amino Acid - chemistry
Receptors, Amino Acid - metabolism
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Summary: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. Proteins 2003. © 2003 Wiley‐Liss, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.10485