Publication Date:
2001-09-05
Description:
We report a flexible strategy for transducing ligand-binding events into electrochemical responses for a wide variety of proteins. The method exploits ligand-mediated hinge-bending motions, intrinsic to the bacterial periplasmic binding protein superfamily, to establish allosterically controlled interactions between electrode surfaces and redox-active, Ru(II)-labeled proteins. This approach allows the development of protein-based bioelectronic interfaces that respond to a diverse set of analytes. Families of these interfaces can be generated either by exploiting natural binding diversity within the superfamily or by reengineering the specificity of individual proteins. These proteins may have numerous medical, environmental, and defense applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benson, D E -- Conrad, D W -- de Lorimier, R M -- Trammell, S A -- Hellinga, H W -- New York, N.Y. -- Science. 2001 Aug 31;293(5535):1641-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Box 3711, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11533486" target="_blank"〉PubMed〈/a〉
Keywords:
Allosteric Regulation
;
Allosteric Site
;
Animals
;
Beer
;
*Biosensing Techniques
;
Blood Glucose/analysis
;
Carrier Proteins/*chemistry/genetics/*metabolism
;
Electrochemistry
;
Electrodes
;
Ligands
;
Maltose/analysis
;
Maltose-Binding Proteins
;
Monosaccharide Transport Proteins/chemistry/metabolism
;
Mutation
;
Oxidation-Reduction
;
Protein Conformation
;
*Protein Engineering
;
Rats
;
*Ruthenium
;
Signal Transduction
;
Thermodynamics
;
Zinc/chemistry/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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