Insight into the stability of the hydrophobic binding proteins of Escherichia coli: Assessing the proteins for use as biosensors
| Autor: | Linda A. Luck, Branka Salopek-Sondi, Derrick Swartz, Matthew C. Skeels |
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| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Protein Denaturation Protein Folding Chemistry Escherichia coli Proteins Biosensing Techniques Periplasmic space Protein unfolding Escherichia coli Leucine specific binding protein Leucine-isoleucine-valine specific binding protein Ligand-dependent conformational stability Ligands Ligand (biochemistry) Biochemistry DNA-binding protein Bacterial Proteins Membrane protein Structural Biology Receptors Amino Acid Protein folding Protein stabilization Isoleucine Carrier Proteins Hydrophobic and Hydrophilic Interactions Molecular Biology Binding domain |
| Popis: | 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 |
| Databáze: | OpenAIRE |
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